Carbonic anhydrase II

Enzyme found in humans

CA2

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes

12CA, 1A42, 1AM6, 1AVN, 1BCD, 1BIC, 1BN1, 1BN3, 1BN4, 1BNM, 1BNN, 1BNQ, 1BNT, 1BNU, 1BNV, 1BNW, 1BV3, 1CA2, 1CA3, 1CAH, 1CAI, 1CAJ, 1CAK, 1CAL, 1CAM, 1CAN, 1CAO, 1CAY, 1CAZ, 1CCS, 1CCT, 1CCU, 1CIL, 1CIM, 1CIN, 1CNB, 1CNC, 1CNG, 1CNH, 1CNI, 1CNJ, 1CNK, 1CNW, 1CNX, 1CNY, 1CRA, 1CVA, 1CVB, 1CVC, 1CVD, 1CVE, 1CVF, 1CVH, 1DCA, 1DCB, 1EOU, 1F2W, 1FQL, 1FQM, 1FQN, 1FQR, 1FR4, 1FR7, 1FSN, 1FSQ, 1FSR, 1G0E, 1G0F, 1G1D, 1G3Z, 1G45, 1G46, 1G48, 1G4J, 1G4O, 1G52, 1G53, 1G54, 1H4N, 1H9N, 1H9Q, 1HCA, 1HEA, 1HEB, 1HEC, 1HED, 1HVA, 1I8Z, 1I90, 1I91, 1I9L, 1I9M, 1I9N, 1I9O, 1I9P, 1I9Q, 1IF4, 1IF5, 1IF6, 1IF7, 1IF8, 1IF9, 1KWQ, 1KWR, 1LG5, 1LG6, 1LGD, 1LUG, 1LZV, 1MOO, 1MUA, 1OKL, 1OKM, 1OKN, 1OQ5, 1RAY, 1RAZ, 1RZA, 1RZB, 1RZC, 1RZD, 1RZE, 1T9N, 1TB0, 1TBT, 1TE3, 1TEQ, 1TEU, 1TG3, 1TG9, 1TH9, 1THK, 1TTM, 1UGA, 1UGB, 1UGC, 1UGD, 1UGE, 1UGF, 1UGG, 1XEG, 1XEV, 1XPZ, 1XQ0, 1YDA, 1YDB, 1YDC, 1YDD, 1YO0, 1YO1, 1YO2, 1Z9Y, 1ZE8, 1ZFK, 1ZFQ, 1ZGE, 1ZGF, 1ZH9, 1ZSA, 1ZSB, 1ZSC, 2ABE, 2AW1, 2AX2, 2CA2, 2CBA, 2CBB, 2CBC, 2CBD, 2CBE, 2EU2, 2EU3, 2EZ7, 2F14, 2FMG, 2FMZ, 2FNK, 2FNM, 2FNN, 2FOQ, 2FOS, 2FOU, 2FOV, 2GD8, 2GEH, 2H15, 2H4N, 2HD6, 2HKK, 2HL4, 2HNC, 2HOC, 2ILI, 2NNG, 2NNO, 2NNS, 2NNV, 2NWO, 2NWP, 2NWY, 2NWZ, 2NXR, 2NXS, 2NXT, 2O4Z, 2OSF, 2OSM, 2POU, 2POV, 2POW, 2Q1B, 2Q1Q, 2Q38, 2QO8, 2QOA, 2QP6, 2VVA, 2VVB, 2WD2, 2WD3, 2WEG, 2WEH, 2WEJ, 2WEO, 2X7S, 2X7T, 2X7U, 3B4F, 3BET, 3BL0, 3BL1, 3C7P, 3CA2, 3CAJ, 3CYU, 3D8W, 3D92, 3D93, 3D9Z, 3DAZ, 3DBU, 3DC3, 3DC9, 3DCC, 3DCS, 3DCW, 3DD0, 3DD8, 3DV7, 3DVB, 3DVC, 3DVD, 3EFI, 3EFT, 3F4X, 3F8E, 3FFP, 3GZ0, 3HFP, 3HKN, 3HKQ, 3HKT, 3HKU, 3HLJ, 3HS4, 3IBI, 3IBL, 3IBN, 3IBU, 3IEO, 3IGP, 3K2F, 3K34, 3K7K, 3KIG, 3KKX, 3KNE, 3KOI, 3KOK, 3KON, 3KS3, 3KWA, 3L14, 3M04, 3M14, 3M1J, 3M1K, 3M1Q, 3M1W, 3M2N, 3M2X, 3M2Y, 3M2Z, 3M3X, 3M40, 3M5E, 3M5S, 3M5T, 3M67, 3M96, 3M98, 3MHC, 3MHI, 3MHL, 3MHM, 3MHO, 3ML2, 3MMF, 3MNA, 3MNH, 3MNI, 3MNJ, 3MNK, 3MNU, 3MWO, 3MYQ, 3MZC, 3N0N, 3N2P, 3N3J, 3N4B, 3NB5, 3NI5, 3NJ9, 3OIK, 3OIL, 3OIM, 3OKU, 3OKV, 3OY0, 3OYQ, 3OYS, 3P3H, 3P3J, 3P44, 3P4V, 3P55, 3P58, 3P5A, 3P5L, 3PJJ, 3PO6, 3PYK, 3QYK, 3R16, 3R17, 3RG3, 3RG4, 3RGE, 3RJ7, 3RLD, 3RYJ, 3RYV, 3RYX, 3RYY, 3RYZ, 3RZ0, 3RZ1, 3RZ5, 3RZ7, 3RZ8, 3S71, 3S72, 3S73, 3S74, 3S75, 3S76, 3S77, 3S78, 3S8X, 3S9T, 3SAP, 3SAX, 3SBH, 3SBI, 3T5U, 3T5Z, 3T82, 3T83, 3T84, 3T85, 3TMJ, 3TVN, 3TVO, 3U3A, 3U45, 3U47, 3U7C, 3V2J, 3V2M, 3V3F, 3V3G, 3V3H, 3V3I, 3V3J, 3V5G, 3V7X, 3VBD, 3ZP9, 4BCW, 4BF1, 4BF6, 4CA2, 4CAC, 4CQ0, 4DZ7, 4DZ9, 4E3D, 4E3F, 4E3G, 4E3H, 4E49, 4E4A, 4E5Q, 4FIK, 4FL7, 4FPT, 4FRC, 4FU5, 4FVN, 4FVO, 4G0C, 4GL1, 4HBA, 4HEW, 4HEY, 4HEZ, 4HF3, 4HT0, 4IDR, 4ILX, 4ITO, 4ITP, 4IWZ, 4JS6, 4JSA, 4JSS, 4JSW, 4JSZ, 4K0S, 4K0T, 4K0Z, 4K13, 4K1Q, 4KAP, 4KNI, 4KNJ, 4KUV, 4KUW, 4KUY, 4KV0, 4L5U, 4L5V, 4L5W, 4LHI, 4LP6, 4M2R, 4M2U, 4M2V, 4M2W, 4MDG, 4MDL, 4MDM, 4MLT, 4MLX, 4MO8, 4MTY, 4N0X, 4N16, 4PQ7, 4PXX, 4PYX, 4PYY, 4PZH, 4Q06, 4Q07, 4Q08, 4Q09, 4Q49, 4Q6D, 4Q6E, 4Q78, 4Q7P, 4Q7S, 4Q7V, 4Q7W, 4Q81, 4Q83, 4Q87, 4Q8X, 4Q8Y, 4Q8Z, 4Q90, 4Q99, 4Q9Y, 4QEF, 4QIY, 4QJM, 4QK1, 4QK2, 4QK3, 4QSA, 4QSB, 4QSI, 4QTL, 4QY3, 4R59, 4R5A, 4R5B, 4RFC, 4RFD, 4RIU, 4RIV, 4RN4, 4RUX, 4RUY, 4RUZ, 4WW6, 4XE1, 4Y0J, 4YGJ, 4YGK, 4YGL, 4YGN, 4Z0Q, 4Z1E, 4Z1J, 4Z1K, 4Z1N, 4ZWI, 4ZWY, 4ZWZ, 5AMD, 5AMG, 5AML, 5BNL, 5BRU, 5BRV, 5BRW, 5BYI, 5CA2, 5CAC, 6CA2, 7CA2, 8CA2, 9CA2, 5E2S, 4YXO, 5CLU, 4YXU, 5EKJ, 5EKH, 1G6V, 5EKM, 4ZX1, 5E2K, 4YYT, 4WL4, 4ZAO, 4ZX0, 4YX4, 4RH2, 4YWP, 4YXI, 5E28, 5E2R, 4ZWX, 5FLT, 5FNH, 5FNJ, 5FLR, 5EH5, 5FLS, 5EHW, 5FNG, 5EH8, 5EHV, 5FNI, 5FNM, 5FNK, 5EH7, 5FLQ, 5FLP, 5FLO, 5DSN, 5DSP, 5J8Z, 5FDC, 4YVY, 5DSM, 5DSL, 5FDI, 5DSJ, 5DSQ, 5DSR, 5C8I, 5DSK, 5G03, 5DSI, 5G0B, 5G0C, 5G01, 5DSO, 5A6H

Identifiers

Aliases

CA2, CA-II, CAC, CAII, Car2, HEL-76, HEL-S-282, Carbonic anhydrase II, carbonic anhydrase 2

External IDs

OMIM: 611492; MGI: 88269; HomoloGene: 37256; GeneCards: CA2; OMA:CA2 - orthologs

Gene location (Human)

Chr.	Chromosome 8 (human)^[1]

Band	8q21.2	Start	85,463,968 bp^[1]
Band	8q21.2	End	85,481,493 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 3 (mouse)^[2]

Band	3 A1\|3 3.23 cM	Start	14,951,333 bp^[2]
Band	3 A1\|3 3.23 cM	End	14,965,830 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

mucosa of colon

mucosa of sigmoid colon

mucosa of transverse colon

rectum

sperm

mucosa of ileum

trabecular bone

jejunal mucosa

pylorus

tibia

Top expressed in

fetal liver hematopoietic progenitor cell

tibiofemoral joint

gastric mucosa

epithelium of stomach

mucous cell of stomach

human fetus

pyloric antrum

choroid plexus of fourth ventricle

deep cerebellar nuclei

left colon

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	zinc ion binding metal ion binding protein binding lyase activity carbonate dehydratase activity arylesterase activity
Cellular component	cytoplasm cytosol membrane myelin sheath apical part of cell plasma membrane microvillus axon basolateral plasma membrane extracellular exosome extracellular space
Biological process	one-carbon metabolic process regulation of chloride transport kidney development response to steroid hormone angiotensin-activated signaling pathway regulation of intracellular pH response to zinc ion positive regulation of osteoclast differentiation positive regulation of bone resorption cellular response to fluid shear stress positive regulation of synaptic transmission, GABAergic response to organic substance secretion response to estrogen morphogenesis of an epithelium odontogenesis of dentin-containing tooth bicarbonate transport positive regulation of cellular pH reduction response to pH regulation of anion transport positive regulation of dipeptide transmembrane transport carbon dioxide transport
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


760


12349

Ensembl


ENSG00000104267


ENSMUSG00000027562

UniProt


P00918


P00920

RefSeq (mRNA)


NM_001293675 NM_000067


NM_009801 NM_001357334

RefSeq (protein)


NP_000058 NP_001280604


NP_033931 NP_001344263

Location (UCSC)

Chr 8: 85.46 – 85.48 Mb

Chr 3: 14.95 – 14.97 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Carbonic anhydrase II (gene name CA2) is one of sixteen forms of human α carbonic anhydrases.^[5] Carbonic anhydrase catalyzes reversible hydration of carbon dioxide. Defects in this enzyme are associated with osteopetrosis and renal tubular acidosis. Renal carbonic anhydrase allows the reabsorption of bicarbonate ions in the proximal tubule. ^[6] Loss of carbonic anhydrase activity in bones impairs the ability of osteoclasts to promote bone resorption, leading to osteopetrosis.^[7]

Interactions

Carbonic anhydrase II has been shown to interact with band 3^[8]^[9]^[10]^[11] and sodium-hydrogen antiporter 1.^[12]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000104267 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000027562 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Frost, S., & McKenna, R. (2014). Carbonic anhydrase : Mechanism, regulation, links to disease, and industrial applications(Subcellular biochemistry). Dordrecht: Springer. doi:10.1007/978-94-007-7359-2
^ "Entrez Gene: CA2 carbonic anhydrase II".
^ Reference, Genetics Home. "Osteopetrosis". Genetics Home Reference. Retrieved 2018-10-31.
^ Sterling, D; Reithmeier R A; Casey J R (December 2001). "A transport metabolon. Functional interaction of carbonic anhydrase II and chloride/bicarbonate exchangers". J. Biol. Chem. 276 (51). United States: 47886–94. doi:10.1074/jbc.M105959200. ISSN 0021-9258. PMID 11606574.
^ Vince, J W; Reithmeier R A (October 1998). "Carbonic anhydrase II binds to the carboxyl terminus of human band 3, the erythrocyte C1-/HCO3- exchanger". J. Biol. Chem. 273 (43). UNITED STATES: 28430–7. doi:10.1074/jbc.273.43.28430. ISSN 0021-9258. PMID 9774471.
^ Vince, J W; Carlsson U; Reithmeier R A (November 2000). "Localization of the Cl-/HCO3- anion exchanger binding site to the amino-terminal region of carbonic anhydrase II". Biochemistry. 39 (44). UNITED STATES: 13344–9. doi:10.1021/bi0015111. ISSN 0006-2960. PMID 11063570.
^ Vince, J W; Reithmeier R A (May 2000). "Identification of the carbonic anhydrase II binding site in the Cl(-)/HCO(3)(-) anion exchanger AE1". Biochemistry. 39 (18). UNITED STATES: 5527–33. doi:10.1021/bi992564p. ISSN 0006-2960. PMID 10820026.
^ Li, Xiuju; Alvarez Bernardo; Casey Joseph R; Reithmeier Reinhart A F; Fliegel Larry (September 2002). "Carbonic anhydrase II binds to and enhances activity of the Na+/H+ exchanger". J. Biol. Chem. 277 (39). United States: 36085–91. doi:10.1074/jbc.M111952200. ISSN 0021-9258. PMID 12138085.

Sly WS, Hu PY (1995). "Human carbonic anhydrases and carbonic anhydrase deficiencies". Annu. Rev. Biochem. 64 (1): 375–401. doi:10.1146/annurev.bi.64.070195.002111. PMID 7574487.
Kumpulainen T (1979). "Immunohistochemical localization of human carbonic anhydrase isoenzyme C.". Histochemistry. 62 (3): 271–80. doi:10.1007/BF00508355. PMID 114507. S2CID 21606492.
Henderson LE, Henriksson D, Nyman PO (1976). "Primary structure of human carbonic anhydrase C." J. Biol. Chem. 251 (18): 5457–63. doi:10.1016/S0021-9258(17)33081-8. PMID 823150.
Hu PY, Roth DE, Skaggs LA, et al. (1993). "A splice junction mutation in intron 2 of the carbonic anhydrase II gene of osteopetrosis patients from Arabic countries". Hum. Mutat. 1 (4): 288–92. doi:10.1002/humu.1380010404. PMID 1301935. S2CID 28188859.
Roth DE, Venta PJ, Tashian RE, Sly WS (1992). "Molecular basis of human carbonic anhydrase II deficiency". Proc. Natl. Acad. Sci. U.S.A. 89 (5): 1804–8. Bibcode:1992PNAS...89.1804R. doi:10.1073/pnas.89.5.1804. PMC 48541. PMID 1542674.
Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
Schwartz GJ, Brion LP, Corey HE, Dorfman HD (1991). "Case report 668. Carbonic anhydrase II deficiency syndrome (osteopetrosis associated with renal tubular acidosis and cerebral calcification)". Skeletal Radiol. 20 (6): 447–52. doi:10.1007/BF00191090. PMID 1925679. S2CID 29176430.
Venta PJ, Welty RJ, Johnson TM, et al. (1991). "Carbonic anhydrase II deficiency syndrome in a Belgian family is caused by a point mutation at an invariant histidine residue (107 His----Tyr): complete structure of the normal human CA II gene". Am. J. Hum. Genet. 49 (5): 1082–90. PMC 1683243. PMID 1928091.
Venta PJ, Tashian RE (1990). "PCR detection of the TAQ1 polymorphism at the CA2 locus". Nucleic Acids Res. 18 (18): 5585. doi:10.1093/nar/18.18.5585. PMC 332284. PMID 1977133.
Sato S, Zhu XL, Sly WS (1990). "Carbonic anhydrase isozymes IV and II in urinary membranes from carbonic anhydrase II-deficient patients". Proc. Natl. Acad. Sci. U.S.A. 87 (16): 6073–6. Bibcode:1990PNAS...87.6073S. doi:10.1073/pnas.87.16.6073. PMC 54474. PMID 2117271.
Kaunisto K, Parkkila S, Tammela T, et al. (1990). "Immunohistochemical localization of carbonic anhydrase isoenzymes in the human male reproductive tract". Histochemistry. 94 (4): 381–6. doi:10.1007/BF00266444. PMID 2121671. S2CID 22668787.
Backman U, Danielsson B, Wistrand PJ (1991). "The excretion of carbonic anhydrase isozymes CA I and CA II in the urine of apparently healthy subjects and in patients with kidney disease". Scand. J. Clin. Lab. Invest. 50 (6): 627–33. doi:10.3109/00365519009089180. PMID 2123360.
Forsman C, Behravan G, Osterman A, Jonsson BH (1989). "Production of active human carbonic anhydrase II in E. coli". Acta Chemica Scandinavica B. 42 (5): 314–8. doi:10.3891/acta.chem.scand.42b-0314. PMID 2850697.
Venta PJ, Montgomery JC, Hewett-Emmett D, Tashian RE (1986). "Comparison of the 5' regions of human and mouse carbonic anhydrase II genes and identification of possible regulatory elements" (PDF). Biochim. Biophys. Acta. 826 (4): 195–201. doi:10.1016/0167-4781(85)90006-5. hdl:2027.42/25466. PMID 3000449.
Ohlsson A, Cumming WA, Paul A, Sly WS (1986). "Carbonic anhydrase II deficiency syndrome: recessive osteopetrosis with renal tubular acidosis and cerebral calcification". Pediatrics. 77 (3): 371–81. doi:10.1542/peds.77.3.371. PMID 3081869. S2CID 33477826.
Nakai H, Byers MG, Venta PJ, et al. (1987). "The gene for human carbonic anhydrase II (CA2) is located at chromosome 8q22". Cytogenet. Cell Genet. 44 (4): 234–5. doi:10.1159/000132378. PMID 3107918.
Montgomery JC, Venta PJ, Tashian RE, Hewett-Emmett D (1987). "Nucleotide sequence of human liver carbonic anhydrase II cDNA". Nucleic Acids Res. 15 (11): 4687. doi:10.1093/nar/15.11.4687. PMC 340889. PMID 3108857.
Murakami H, Marelich GP, Grubb JH, et al. (1988). "Cloning, expression, and sequence homologies of cDNA for human carbonic anhydrase II". Genomics. 1 (2): 159–66. doi:10.1016/0888-7543(87)90008-5. PMID 3121496.
Eriksson AE, Jones TA, Liljas A (1989). "Refined structure of human carbonic anhydrase II at 2.0 A resolution". Proteins. 4 (4): 274–82. doi:10.1002/prot.340040406. PMID 3151019. S2CID 25590322.
Eriksson AE, Kylsten PM, Jones TA, Liljas A (1989). "Crystallographic studies of inhibitor binding sites in human carbonic anhydrase II: a pentacoordinated binding of the SCN- ion to the zinc at high pH". Proteins. 4 (4): 283–93. doi:10.1002/prot.340040407. PMID 3151020. S2CID 25849532.

PDB gallery

12ca: ALTERING THE MOUTH OF A HYDROPHOBIC POCKET. STRUCTURE AND KINETICS OF HUMAN CARBONIC ANHYDRASE II MUTANTS AT RESIDUE VAL-121
1a42: HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH BRINZOLAMIDE
1am6: CARBONIC ANHYDRASE II INHIBITOR: ACETOHYDROXAMATE
1avn: HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH THE HISTAMINE ACTIVATOR
1bcd: X-RAY CRYSTALLOGRAPHIC STRUCTURE OF A COMPLEX BETWEEN HUMAN CARBONIC ANHYDRASE II AND A NEW TOPICAL INHIBITOR, TRIFLUOROMETHANE SULPHONAMIDE
1bic: CRYSTALLOGRAPHIC ANALYSIS OF THR-200-> HIS HUMAN CARBONIC ANHYDRASE II AND ITS COMPLEX WITH THE SUBSTRATE, HCO3-
1bn1: CARBONIC ANHYDRASE II INHIBITOR
1bn3: CARBONIC ANHYDRASE II INHIBITOR
1bn4: CARBONIC ANHYDRASE II INHIBITOR
1bnm: CARBONIC ANHYDRASE II INHIBITOR
1bnn: CARBONIC ANHYDRASE II INHIBITOR
1bnq: CARBONIC ANHYDRASE II INHIBITOR
1bnt: CARBONIC ANHYDRASE II INHIBITOR
1bnu: CARBONIC ANHYDRASE II INHIBITOR
1bnv: CARBONIC ANHYDRASE II INHIBITOR
1bnw: CARBONIC ANHYDRASE II INHIBITOR
1bv3: HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH UREA
1ca2: REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE II AT 2.0 ANGSTROMS RESOLUTION
1ca3: UNEXPECTED PH-DEPENDENT CONFORMATION OF HIS-64, THE PROTON SHUTTLE OF CARBONIC ANHYDRASE II.
1cah: STRUCTURE OF COBALT CARBONIC ANHYDRASE COMPLEXED WITH BICARBONATE
1cai: STRUCTURAL ANALYSIS OF THE ZINC HYDROXIDE-THR 199-GLU 106 HYDROGEN BONDING NETWORK IN HUMAN CARBONIC ANHYDRASE II
1caj: STRUCTURAL ANALYSIS OF THE ZINC HYDROXIDE-THR 199-GLU 106 HYDROGEN BONDING NETWORK IN HUMAN CARBONIC ANHYDRASE II
1cak: STRUCTURAL ANALYSIS OF THE ZINC HYDROXIDE-THR 199-GLU 106 HYDROGEN BONDING NETWORK IN HUMAN CARBONIC ANHYDRASE II
1cal: STRUCTURAL ANALYSIS OF THE ZINC HYDROXIDE-THR 199-GLU 106 HYDROGEN BONDING NETWORK IN HUMAN CARBONIC ANHYDRASE II
1cam: STRUCTURAL ANALYSIS OF THE ZINC HYDROXIDE-THR 199-GLU 106 HYDROGEN BONDING NETWORK IN HUMAN CARBONIC ANHYDRASE II
1can: CRYSTALLOGRAPHIC STUDIES OF THE BINDING OF PROTONATED AND UNPROTONATED INHIBITORS TO CARBONIC ANHYDRASE USING HYDROGEN SULPHIDE AND NITRATE ANIONS
1cao: CRYSTALLOGRAPHIC STUDIES OF THE BINDING OF PROTONATED AND UNPROTONATED INHIBITORS TO CARBONIC ANHYDRASE USING HYDROGEN SULPHIDE AND NITRATE ANIONS
1cay: WILD-TYPE AND E106Q MUTANT CARBONIC ANHYDRASE COMPLEXED WITH ACETATE
1caz: WILD-TYPE AND E106Q MUTANT CARBONIC ANHYDRASE COMPLEXED WITH ACETATE
1ccs: STRUCTURE-ASSISTED REDESIGN OF A PROTEIN-ZINC BINDING SITE WITH FEMTOMOLAR AFFINITY
1cct: STRUCTURE-ASSISTED REDESIGN OF A PROTEIN-ZINC BINDING SITE WITH FEMTOMOLAR AFFINITY
1ccu: STRUCTURE-ASSISTED REDESIGN OF A PROTEIN-ZINC BINDING SITE WITH FEMTOMOLAR AFFINITY
1cil: THE POSITIONS OF HIS-64 AND A BOUND WATER IN HUMAN CARBONIC ANHYDRASE II UPON BINDING THREE STRUCTURALLY RELATED INHIBITORS
1cim: THE POSITIONS OF HIS-64 AND A BOUND WATER IN HUMAN CARBONIC ANHYDRASE II UPON BINDING THREE STRUCTURALLY RELATED INHIBITORS
1cin: THE POSITIONS OF HIS-64 AND A BOUND WATER IN HUMAN CARBONIC ANHYDRASE II UPON BINDING THREE STRUCTURALLY RELATED INHIBITORS
1cnb: COMPENSATORY PLASTIC EFFECTS IN THE REDESIGN OF PROTEIN-ZINC BINDING SITES
1cnc: COMPENSATORY PLASTIC EFFECTS IN THE REDESIGN OF PROTEIN-ZINC BINDING SITES
1cng: X-RAY CRYSTALLOGRAPHIC STUDIES OF ENGINEERED HYDROGEN BOND NETWORKS IN A PROTEIN-ZINC BINDING SITE
1cnh: X-RAY CRYSTALLOGRAPHIC STUDIES OF ENGINEERED HYDROGEN BOND NETWORKS IN A PROTEIN-ZINC BINDING SITE
1cni: X-RAY CRYSTALLOGRAPHIC STUDIES OF ENGINEERED HYDROGEN BOND NETWORKS IN A PROTEIN-ZINC BINDING SITE
1cnj: X-RAY CRYSTALLOGRAPHIC STUDIES OF ENGINEERED HYDROGEN BOND NETWORKS IN A PROTEIN-ZINC BINDING SITE
1cnk: X-RAY CRYSTALLOGRAPHIC STUDIES OF ENGINEERED HYDROGEN BOND NETWORKS IN A PROTEIN-ZINC BINDING SITE
1cnw: SECONDARY INTERACTIONS SIGNIFICANTLY REMOVED FROM THE SULFONAMIDE BINDING POCKET OF CARBONIC ANHYDRASE II INFLUENCE BINDING CONSTANTS
1cnx: SECONDARY INTERACTIONS SIGNIFICANTLY REMOVED FROM THE SULFONAMIDE BINDING POCKET OF CARBONIC ANHYDRASE II INFLUENCE BINDING CONSTANTS
1cny: SECONDARY INTERACTIONS SIGNIFICANTLY REMOVED FROM THE SULFONAMIDE BINDING POCKET OF CARBONIC ANHYDRASE II INFLUENCE BINDING CONSTANTS
1cra: THE COMPLEX BETWEEN HUMAN CARBONIC ANHYDRASE II AND THE AROMATIC INHIBITOR 1,2,4-TRIAZOLE
1cva: STRUCTURAL AND FUNCTIONAL IMPORTANCE OF A CONSERVED HYDROGEN BOND NETWORK IN HUMAN CARBONIC ANHYDRASE II
1cvb: STRUCTURAL AND FUNCTIONAL IMPORTANCE OF A CONSERVED HYDROGEN BOND NETWORK IN HUMAN CARBONIC ANHYDRASE II
1cvc: REDESIGNING THE ZINC BINDING SITE OF HUMAN CARBONIC ANHYDRASE II: STRUCTURE OF A HIS2ASP-ZN2+ METAL COORDINATION POLYHEDRON
1cvd: STRUCTURAL CONSEQUENCES OF REDESIGNING A PROTEIN-ZINC BINDING SITE
1cve: STRUCTURAL CONSEQUENCES OF REDESIGNING A PROTEIN-ZINC BINDING SITE
1cvf: STRUCTURAL CONSEQUENCES OF REDESIGNING A PROTEIN-ZINC BINDING SITE
1cvh: STRUCTURAL CONSEQUENCES OF REDESIGNING A PROTEIN-ZINC BINDING SITE
1dca: STRUCTURE OF AN ENGINEERED METAL BINDING SITE IN HUMAN CARBONIC ANHYDRASE II REVEALS THE ARCHITECTURE OF A REGULATORY CYSTEINE SWITCH
1dcb: STRUCTURE OF AN ENGINEERED METAL BINDING SITE IN HUMAN CARBONIC ANHYDRASE II REVEALS THE ARCHITECTURE OF A REGULATORY CYSTEINE SWITCH
1eou: CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH AN ANTICONVULSANT SUGAR SULFAMATE
1f2w: THE MECHANISM OF CYANAMIDE HYDRATION CATALYZED BY CARBONIC ANHYDRASE II REVEALED BY CRYOGENIC X-RAY DIFFRACTION
1fql: X-RAY CRYSTAL STRUCTURE OF ZINC-BOUND F95M/W97V CARBONIC ANHYDRASE (CAII) VARIANT
1fqm: X-RAY CRYSTAL STRUCTURE OF ZINC-BOUND F93I/F95M/W97V CARBONIC ANHYDRASE (CAII) VARIANT
1fqn: X-RAY CRYSTAL STRUCTURE OF METAL-FREE F93I/F95M/W97V CARBONIC ANHYDRASE (CAII) VARIANT
1fqr: X-RAY CRYSTAL STRUCTURE OF COBALT-BOUND F93I/F95M/W97V CARBONIC ANHYDRASE (CAII) VARIANT
1fr4: X-RAY CRYSTAL STRUCTURE OF COPPER-BOUND F93I/F95M/W97V CARBONIC ANHYDRASE (CAII) VARIANT
1fr7: X-RAY CRYSTAL STRUCTURE OF ZINC-BOUND F93S/F95L/W97M CARBONIC ANHYDRASE (CAII) VARIANT
1fsn: X-RAY CRYSTAL STRUCTURE OF METAL-FREE F93S/F95L/W97M CARBONIC ANHYDRASE (CAII) VARIANT
1fsq: X-RAY CRYSTAL STRUCTURE OF COBALT-BOUND F93S/F95L/W97M CARBONIC ANHYDRASE (CAII) VARIANT
1fsr: X-RAY CRYSTAL STRUCTURE OF COPPER-BOUND F93S/F95L/W97M CARBONIC ANHYDRASE (CAII) VARIANT
1g0e: SITE-SPECIFIC MUTANT (HIS64 REPLACED WITH ALA) OF HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH 4-METHYLIMIDAZOLE
1g0f: SITE-SPECIFIC MUTANT (HIS64 REPLACED WITH ALA) OF HUMAN CARBONIC ANHYDRASE II
1g1d: CARBONIC ANHYDRASE II COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2-FLUOROPHENYL)METHYL]-BENZAMIDE
1g3z: CARBONIC ANHYDRASE II (F131V)
1g45: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2-FLUOROPHENYL)METHYL]-BENZAMIDE
1g46: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3-DIFLUOROPHENYL)METHYL]-BENZAMIDE
1g48: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,6-DIFLUOROPHENYL)METHYL]-BENZAMIDE
1g4j: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3,4,5,6-PENTAFLUOROPHENYL)METHYL]-BENZAMIDE
1g4o: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-PHENYLMETHYLBENZAMIDE
1g52: CARBONIC ANHYDRASE II COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3-DIFLUOROPHENYL)METHYL]-BENZAMIDE
1g53: CARBONIC ANHYDRASE II COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,6-DIFLUOROPHENYL)METHYL]-BENZAMIDE
1g54: CARBONIC ANHYDRASE II COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3,4,5,6-PENTAFLUOROPHENYL)METHYL]-BENZAMIDE
1g6v: Complex of the camelid heavy-chain antibody fragment CAB-CA05 with bovine carbonic anhydrase
1h4n: H94N CARBONIC ANHYDRASE II COMPLEXED WITH TRIS
1h9n: H119N CARBONIC ANHYDRASE II
1h9q: H119Q CARBONIC ANHYDRASE II
1hca: UNEXPECTED PH-DEPENDENT CONFORMATION OF HIS-64, THE PROTON SHUTTLE OF CARBONIC ANHYDRASE II.
1hea: CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (HCA II) (E.C.4.2.1.1) MUTANT WITH LEU 198 REPLACED BY ARG (L198R)
1heb: STRUCTURAL CONSEQUENCES OF HYDROPHILIC AMINO-ACID SUBSTITUTIONS IN THE HYDROPHOBIC POCKET OF HUMAN CARBONIC ANHYDRASE II
1hec: STRUCTURAL CONSEQUENCES OF HYDROPHILIC AMINO-ACID SUBSTITUTIONS IN THE HYDROPHOBIC POCKET OF HUMAN CARBONIC ANHYDRASE II
1hed: STRUCTURAL CONSEQUENCES OF HYDROPHILIC AMINO-ACID SUBSTITUTIONS IN THE HYDROPHOBIC POCKET OF HUMAN CARBONIC ANHYDRASE II
1hva: ENGINEERING THE ZINC BINDING SITE OF HUMAN CARBONIC ANHYDRASE II: STRUCTURE OF THE HIS-94-> CYS APOENZYME IN A NEW CRYSTALLINE FORM
1i8z: CARBONIC ANHYDRASE II COMPLEXED WITH AL-6629 2H-THIENO[3,2-E]-1,2-THIAZINE-6-SULFONAMIDE, 2-(3-METHOXYPHENYL)-3-(4-MORPHOLINYL)-, 1,1-DIOXIDE
1i90: CARBONIC ANHYDRASE II COMPLEXED WITH AL-8520 2H-THIENO[3,2-E]-1,2-THIAZINE-6-SULFONAMIDE, 4-AMINO-3,4-DIHYDRO-2-(3-METHOXYPROPYL)-, 1,1-DIOXIDE, (R)
1i91: CARBONIC ANHYDRASE II COMPLEXED WITH AL-6619 2H-THIENO[3,2-E]-1,2-THIAZINE-6-SULFONAMIDE, 2-(3-HYDROXYPHENYL)-3-(4-MORPHOLINYL)-, 1,1-DIOXIDE
1i9l: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(4-FLUOROPHENYL)METHYL]-BENZAMIDE
1i9m: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,4-DIFLUOROPHENYL)METHYL]-BENZAMIDE
1i9n: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,5-DIFLUOROPHENYL)METHYL]-BENZAMIDE
1i9o: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3,4-TRIFLUOROPHENYL)METHYL]-BENZAMIDE
1i9p: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,4,6-TRIFLUOROPHENYL)METHYL]-BENZAMIDE
1i9q: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(3,4,5-TRIFLUOROPHENYL)METHYL]-BENZAMIDE
1if4: Carbonic Anhydrase II Complexed With 4-fluorobenzenesulfonamide
1if5: Carbonic Anhydrase II Complexed With 2,6-difluorobenzenesulfonamide
1if6: Carbonic Anhydrase II Complexed With 3,5-difluorobenzenesulfonamide
1if7: Carbonic Anhydrase II Complexed With (R)-N-(3-Indol-1-yl-2-methyl-propyl)-4-sulfamoyl-benzamide
1if8: Carbonic Anhydrase II Complexed With (S)-N-(3-Indol-1-yl-2-methyl-propyl)-4-sulfamoyl-benzamide
1if9: Carbonic Anhydrase II Complexed With N-[2-(1H-Indol-5-yl)-butyl]-4-sulfamoyl-benzamide
1kwq: HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH INHIBITOR 2000-07
1kwr: HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH INHIBITOR 0134-36
1lg5: Crystal Structure Analysis of the HCA II Mutant T199P in complex with beta-mercaptoethanol
1lg6: Crystal Structure Analysis of HCA II Mutant T199P in Complex with Thiocyanate
1lgd: Crystal Structure Analysis of HCA II Mutant T199P in Complex with Bicarbonate
1lug: Full Matrix Error Analysis of Carbonic Anhydrase
1lzv: Site-Specific Mutant (Tyr7 replaced with His) of Human Carbonic Anhydrase II
1moo: Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at high resolution
1mua: STRUCTURE AND ENERGETICS OF A NON-PROLINE CIS-PEPTIDYL LINKAGE IN AN ENGINEERED PROTEIN
1okl: CARBONIC ANHYDRASE II COMPLEX WITH THE 1OKL INHIBITOR 5-DIMETHYLAMINO-NAPHTHALENE-1-SULFONAMIDE
1okm: CARBONIC ANHYDRASE II COMPLEX WITH THE 1OKM INHIBITOR 4-SULFONAMIDE-[1-(4-AMINOBUTANE)]BENZAMIDE
1okn: CARBONIC ANHYDRASE II COMPLEX WITH THE 1OKN INHIBITOR 4-SULFONAMIDE-[1-(4-N-(5-FLUORESCEIN THIOUREA)BUTANE)]
1oq5: CARBONIC ANHYDRASE II IN COMPLEX WITH NANOMOLAR INHIBITOR
1ray: THE STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH BROMIDE AND AZIDE
1raz: THE STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH BROMIDE AND AZIDE
1rza: X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES
1rzb: X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES
1rzc: X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES
1rzd: X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES
1rze: X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES
1t9n: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II
1tb0: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II
1tbt: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II
1te3: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II
1teq: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II
1teu: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II
1tg3: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II
1tg9: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II
1th9: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II
1thk: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II
1ttm: Human carbonic anhydrase II complexed with 667-coumate
1uga: HUMAN CARBONIC ANHYDRASE II[HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY PHE (A65F)
1ugb: HUMAN CARBONIC ANHYDRASE II[HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY GLY (A65G)
1ugc: HUMAN CARBONIC ANHYDRASE II [HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY HIS (A65H)
1ugd: HUMAN CARBONIC ANHYDRASE II[HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY SER (A65S)
1uge: HUMAN CARBONIC ANHYDRASE II [HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY LEU (A65L)
1ugf: HUMAN CARBONIC ANHYDRASE II [HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY THR (A65T)
1ugg: HUMAN CARBONIC ANHYDRASE II[HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY SER (A65S)-ORTHORHOMBIC FORM
1xeg: Crystal structure of human carbonic anhydrase II complexed with an acetate ion
1xev: Crystal structure of human carbonic anhydrase II in a new crystal form
1xpz: Structure of human carbonic anhydrase II with 4-[4-O-sulfamoylbenzyl)(4-cyanophenyl)amino]-4H-[1,2,4]-triazole
1xq0: Structure of human carbonic anhydrase II with 4-[(3-bromo-4-O-sulfamoylbenzyl)(4-cyanophenyl)amino]-4H-[1,2,4]-triazole
1yda: STRUCTURAL BASIS OF INHIBITOR AFFINITY TO VARIANTS OF HUMAN CARBONIC ANHYDRASE II
1ydb: STRUCTURAL BASIS OF INHIBITOR AFFINITY TO VARIANTS OF HUMAN CARBONIC ANHYDRASE II
1ydc: STRUCTURAL BASIS OF INHIBITOR AFFINITY TO VARIANTS OF HUMAN CARBONIC ANHYDRASE II
1ydd: STRUCTURAL BASIS OF INHIBITOR AFFINITY TO VARIANTS OF HUMAN CARBONIC ANHYDRASE II
1yo0: Proton Transfer from His200 in Human Carbonic Anhydrase II
1yo1: Proton Transfer from His200 in Human Carbonic Anhydrase II
1yo2: Proton Transfer from His200 in Human Carbonic Anhydrase II
1z9y: carbonic anhydrase II in complex with furosemide as sulfonamide inhibitor
1ze8: Carbonic anhydrase II in complex with a membrane-impermeant sulfonamide inhibitor
1zfk: carbonic anhydrase II in complex with N-4-sulfonamidphenyl-N'-4-methylbenzosulfonylurease as sulfonamide inhibitor
1zfq: carbonic anhydrase II in complex with ethoxzolamidphenole as sulfonamide inhibitor
1zge: carbonic anhydrase II in complex with p-Sulfonamido-o,o'-dichloroaniline as sulfonamide inhibitor
1zgf: carbonic anhydrase II in complex with trichloromethiazide as sulfonamide inhibitor
1zh9: carbonic anhydrase II in complex with N-4-Methyl-1-piperazinyl-N'-(p-sulfonamide)phenylthiourea as sulfonamide inhibitor
1zsa: CARBONIC ANHYDRASE II MUTANT E117Q, APO FORM
1zsb: CARBONIC ANHYDRASE II MUTANT E117Q, TRANSITION STATE ANALOGUE ACETAZOLAMIDE
1zsc: CARBONIC ANHYDRASE II MUTANT E117Q, HOLO FORM
2abe: Carbonic anhydrase activators: X-ray crystal structure of the adduct of human isozyme II with L-histidine as a platform for the design of stronger activators
2aw1: Carbonic anhydrase inhibitors: Valdecoxib binds to a different active site region of the human isoform II as compared to the structurally related cyclooxygenase II ""selective"" inhibitor Celecoxib
2ax2: Production and X-ray crystallographic analysis of fully deuterated human carbonic anhydrase II
2ca2: CRYSTALLOGRAPHIC STUDIES OF INHIBITOR BINDING SITES IN HUMAN CARBONIC ANHYDRASE II. A PENTACOORDINATED BINDING OF THE SCN-ION TO THE ZINC AT HIGH P*H
2cba: STRUCTURE OF NATIVE AND APO CARBONIC ANHYDRASE II AND SOME OF ITS ANION-LIGAND COMPLEXES
2cbb: STRUCTURE OF NATIVE AND APO CARBONIC ANHYDRASE II AND SOME OF ITS ANION-LIGAND COMPLEXES
2cbc: STRUCTURE OF NATIVE AND APO CARBONIC ANHYDRASE II AND SOME OF ITS ANION-LIGAND COMPLEXES
2cbd: STRUCTURE OF NATIVE AND APO CARBONIC ANHYDRASE II AND SOME OF ITS ANION-LIGAND COMPLEXES
2cbe: STRUCTURE OF NATIVE AND APO CARBONIC ANHYDRASE II AND SOME OF ITS ANION-LIGAND COMPLEXES
2eu2: Human Carbonic Anhydrase II in complex with novel inhibitors
2eu3: Human Carbonic anhydrase II in complex with novel inhibitors
2ez7: Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII and XIV with L- and D-histidine and crystallographic analysis of their adducts with isoform II: engineering proton transfer processes within the active site of an enzyme
2f14: The Crystal Structure of the Human Carbonic Anhydrase II in Complex with a Fluorescent Inhibitor
2fmg: Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII and XIV with L- and D- phenylalanine and crystallographic analysis of their adducts with isozyme II: sterospecific recognition within the active site of an enzyme and its consequences for the drug design, structure with L-phenylalanine
2fmz: Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII and XIV with L- and D- phenylalanine, structure with D-Phenylalanine.
2fnk: Activation of Human Carbonic Anhydrase II by exogenous proton donors
2fnm: Activation of human carbonic anhdyrase II by exogenous proton donors
2fnn: Activation of human carbonic anhydrase II by exogenous proton donors
2foq: Human Carbonic Anhydrase II complexed with two-prong inhibitors
2fos: Human Carbonic Anhydrase II complexed with two-prong inhibitors
2fou: Human Carbonic Anhydrase II complexed with two-prong inhibitors
2fov: Human Carbonic Anhydrase II complexed with two-prong inhibitors
2gd8: Crystal structure analysis of the human carbonic anhydrase II in complex with a 2-substituted estradiol bis-sulfamate
2geh: N-Hydroxyurea, a versatile zinc binding function in the design of metalloenzyme inhibitors
2h15: Carbonic anhydrase inhibitors: Clashing with Ala65 as a means of designing isozyme-selective inhibitors that show low affinity for the ubiquitous isozyme II
2h4n: H94N CARBONIC ANHYDRASE II COMPLEXED WITH ACETAZOLAMIDE
2hd6: Crystal structure of the human carbonic anhydrase II in complex with a hypoxia-activatable sulfonamide.
2hkk: Carbonic anhydrase activators: Solution and X-ray crystallography for the interaction of andrenaline with various carbonic anhydrase isoforms
2hl4: Crystal structure analysis of human carbonic anhydrase II in complex with a benzenesulfonamide derivative
2hnc: Crystal structure of the human carbonic anhydrase II in complex with the 5-amino-1,3,4-thiadiazole-2-sulfonamide inhibitor.
2hoc: Crystal structure of the human carbonic anhydrase II in complex with the 5-(4-amino-3-chloro-5-fluorophenylsulfonamido)-1,3,4-thiadiazole-2-sulfonamide inhibitor
2ili: Refine atomic structure of human carbonic anhydrase II
2nng: Structure of inhibitor binding to Carbonic Anhydrase II
2nno: Structure of inhibitor binding to Carbonic Anhydrase II
2nns: Structure of inhibitor binding to Carbonic Anhydrase II
2nnv: Structure of inhibitor binding to Carbonic Anhydrase II
2nwo: Structural and kinetic effect of hydrophobic mutations in the active site of human carbonic anhydrase II
2nwp: Structural and kinetic effects of hydrophobic mutations in the active site of human carbonic anhydrase II
2nwy: Structural and kinetic effects of hydrophobic mutations on the active site of human carbonic anhydrase II
2nwz: Structural and kinetic effects of hydrophobic mutations on the active site of human carbonic anhydrase II
2nxr: Structural effects of hydrophobic mutations on the active site of human carbonic anhydrase II
2nxs: Structural and kinetic effects of hydrophobic mutations in the active site of human carbonic anhydrase II
2nxt: Structural and kinetic effects of hydrophobic mutations in the active site of human carbonic anhydrase II
2o4z: Crystal structure of the Carbonic Anhydrase II complexed with hydroxysulfamide inhibitor
3ca2: CRYSTALLOGRAPHIC STUDIES OF INHIBITOR BINDING SITES IN HUMAN CARBONIC ANHYDRASE II. A PENTACOORDINATED BINDING OF THE SCN-ION TO THE ZINC AT HIGH P*H
4ca2: ENGINEERING THE HYDROPHOBIC POCKET OF CARBONIC ANHYDRASE II
4cac: REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE II AT 2.0 ANGSTROMS RESOLUTION
5ca2: CONFORMATIONAL MOBILITY OF HIS-64 IN THE THR-200 (RIGHT ARROW) SER MUTANT OF HUMAN CARBONIC ANHYDRASE II
5cac: REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE II AT 2.0 ANGSTROMS RESOLUTION
6ca2: ENGINEERING THE HYDROPHOBIC POCKET OF CARBONIC ANHYDRASE II
7ca2: ENGINEERING THE HYDROPHOBIC POCKET OF CARBONIC ANHYDRASE II
8ca2: ENGINEERING THE HYDROPHOBIC POCKET OF CARBONIC ANHYDRASE II
9ca2: ENGINEERING THE HYDROPHOBIC POCKET OF CARBONIC ANHYDRASE II