Carbonic anhydrase II

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, 5A6H76012349ENSG00000104267ENSMUSG00000027562P00918P00920NM_001293675NM_000067NM_009801NM_001357334NP_000058NP_001280604NP_033931NP_001344263Carbonic anhydrase II (gene name CA2), is one of sixteen forms of human α carbonic anhydrases . 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. Loss of carbonic anhydrase activity in bones impairs the ability of osteoclasts to promote bone resorption, leading to osteopetrosis. 12ca: ALTERING THE MOUTH OF A HYDROPHOBIC POCKET. STRUCTURE AND KINETICS OF HUMAN CARBONIC ANHYDRASE II MUTANTS AT RESIDUE VAL-1211a42: HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH BRINZOLAMIDE1am6: CARBONIC ANHYDRASE II INHIBITOR: ACETOHYDROXAMATE1avn: HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH THE HISTAMINE ACTIVATOR1bcd: X-RAY CRYSTALLOGRAPHIC STRUCTURE OF A COMPLEX BETWEEN HUMAN CARBONIC ANHYDRASE II AND A NEW TOPICAL INHIBITOR, TRIFLUOROMETHANE SULPHONAMIDE1bic: CRYSTALLOGRAPHIC ANALYSIS OF THR-200-> HIS HUMAN CARBONIC ANHYDRASE II AND ITS COMPLEX WITH THE SUBSTRATE, HCO3-1bn1: CARBONIC ANHYDRASE II INHIBITOR1bn3: CARBONIC ANHYDRASE II INHIBITOR1bn4: CARBONIC ANHYDRASE II INHIBITOR1bnm: CARBONIC ANHYDRASE II INHIBITOR1bnn: CARBONIC ANHYDRASE II INHIBITOR1bnq: CARBONIC ANHYDRASE II INHIBITOR1bnt: CARBONIC ANHYDRASE II INHIBITOR1bnu: CARBONIC ANHYDRASE II INHIBITOR1bnv: CARBONIC ANHYDRASE II INHIBITOR1bnw: CARBONIC ANHYDRASE II INHIBITOR1bv3: HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH UREA1ca2: REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE II AT 2.0 ANGSTROMS RESOLUTION1ca3: UNEXPECTED PH-DEPENDENT CONFORMATION OF HIS-64, THE PROTON SHUTTLE OF CARBONIC ANHYDRASE II.1cah: STRUCTURE OF COBALT CARBONIC ANHYDRASE COMPLEXED WITH BICARBONATE1cai: STRUCTURAL ANALYSIS OF THE ZINC HYDROXIDE-THR 199-GLU 106 HYDROGEN BONDING NETWORK IN HUMAN CARBONIC ANHYDRASE II1caj: STRUCTURAL ANALYSIS OF THE ZINC HYDROXIDE-THR 199-GLU 106 HYDROGEN BONDING NETWORK IN HUMAN CARBONIC ANHYDRASE II1cak: STRUCTURAL ANALYSIS OF THE ZINC HYDROXIDE-THR 199-GLU 106 HYDROGEN BONDING NETWORK IN HUMAN CARBONIC ANHYDRASE II1cal: STRUCTURAL ANALYSIS OF THE ZINC HYDROXIDE-THR 199-GLU 106 HYDROGEN BONDING NETWORK IN HUMAN CARBONIC ANHYDRASE II1cam: STRUCTURAL ANALYSIS OF THE ZINC HYDROXIDE-THR 199-GLU 106 HYDROGEN BONDING NETWORK IN HUMAN CARBONIC ANHYDRASE II1can: CRYSTALLOGRAPHIC STUDIES OF THE BINDING OF PROTONATED AND UNPROTONATED INHIBITORS TO CARBONIC ANHYDRASE USING HYDROGEN SULPHIDE AND NITRATE ANIONS1cao: CRYSTALLOGRAPHIC STUDIES OF THE BINDING OF PROTONATED AND UNPROTONATED INHIBITORS TO CARBONIC ANHYDRASE USING HYDROGEN SULPHIDE AND NITRATE ANIONS1cay: WILD-TYPE AND E106Q MUTANT CARBONIC ANHYDRASE COMPLEXED WITH ACETATE1caz: WILD-TYPE AND E106Q MUTANT CARBONIC ANHYDRASE COMPLEXED WITH ACETATE1ccs: STRUCTURE-ASSISTED REDESIGN OF A PROTEIN-ZINC BINDING SITE WITH FEMTOMOLAR AFFINITY1cct: STRUCTURE-ASSISTED REDESIGN OF A PROTEIN-ZINC BINDING SITE WITH FEMTOMOLAR AFFINITY1ccu: STRUCTURE-ASSISTED REDESIGN OF A PROTEIN-ZINC BINDING SITE WITH FEMTOMOLAR AFFINITY1cil: THE POSITIONS OF HIS-64 AND A BOUND WATER IN HUMAN CARBONIC ANHYDRASE II UPON BINDING THREE STRUCTURALLY RELATED INHIBITORS1cim: THE POSITIONS OF HIS-64 AND A BOUND WATER IN HUMAN CARBONIC ANHYDRASE II UPON BINDING THREE STRUCTURALLY RELATED INHIBITORS1cin: THE POSITIONS OF HIS-64 AND A BOUND WATER IN HUMAN CARBONIC ANHYDRASE II UPON BINDING THREE STRUCTURALLY RELATED INHIBITORS1cnb: COMPENSATORY PLASTIC EFFECTS IN THE REDESIGN OF PROTEIN-ZINC BINDING SITES1cnc: COMPENSATORY PLASTIC EFFECTS IN THE REDESIGN OF PROTEIN-ZINC BINDING SITES1cng: X-RAY CRYSTALLOGRAPHIC STUDIES OF ENGINEERED HYDROGEN BOND NETWORKS IN A PROTEIN-ZINC BINDING SITE1cnh: X-RAY CRYSTALLOGRAPHIC STUDIES OF ENGINEERED HYDROGEN BOND NETWORKS IN A PROTEIN-ZINC BINDING SITE1cni: X-RAY CRYSTALLOGRAPHIC STUDIES OF ENGINEERED HYDROGEN BOND NETWORKS IN A PROTEIN-ZINC BINDING SITE1cnj: X-RAY CRYSTALLOGRAPHIC STUDIES OF ENGINEERED HYDROGEN BOND NETWORKS IN A PROTEIN-ZINC BINDING SITE1cnk: X-RAY CRYSTALLOGRAPHIC STUDIES OF ENGINEERED HYDROGEN BOND NETWORKS IN A PROTEIN-ZINC BINDING SITE1cnw: SECONDARY INTERACTIONS SIGNIFICANTLY REMOVED FROM THE SULFONAMIDE BINDING POCKET OF CARBONIC ANHYDRASE II INFLUENCE BINDING CONSTANTS1cnx: SECONDARY INTERACTIONS SIGNIFICANTLY REMOVED FROM THE SULFONAMIDE BINDING POCKET OF CARBONIC ANHYDRASE II INFLUENCE BINDING CONSTANTS1cny: SECONDARY INTERACTIONS SIGNIFICANTLY REMOVED FROM THE SULFONAMIDE BINDING POCKET OF CARBONIC ANHYDRASE II INFLUENCE BINDING CONSTANTS1cra: THE COMPLEX BETWEEN HUMAN CARBONIC ANHYDRASE II AND THE AROMATIC INHIBITOR 1,2,4-TRIAZOLE1cva: STRUCTURAL AND FUNCTIONAL IMPORTANCE OF A CONSERVED HYDROGEN BOND NETWORK IN HUMAN CARBONIC ANHYDRASE II1cvb: STRUCTURAL AND FUNCTIONAL IMPORTANCE OF A CONSERVED HYDROGEN BOND NETWORK IN HUMAN CARBONIC ANHYDRASE II1cvc: REDESIGNING THE ZINC BINDING SITE OF HUMAN CARBONIC ANHYDRASE II: STRUCTURE OF A HIS2ASP-ZN2+ METAL COORDINATION POLYHEDRON1cvd: STRUCTURAL CONSEQUENCES OF REDESIGNING A PROTEIN-ZINC BINDING SITE1cve: STRUCTURAL CONSEQUENCES OF REDESIGNING A PROTEIN-ZINC BINDING SITE1cvf: STRUCTURAL CONSEQUENCES OF REDESIGNING A PROTEIN-ZINC BINDING SITE1cvh: STRUCTURAL CONSEQUENCES OF REDESIGNING A PROTEIN-ZINC BINDING SITE1dca: STRUCTURE OF AN ENGINEERED METAL BINDING SITE IN HUMAN CARBONIC ANHYDRASE II REVEALS THE ARCHITECTURE OF A REGULATORY CYSTEINE SWITCH1dcb: STRUCTURE OF AN ENGINEERED METAL BINDING SITE IN HUMAN CARBONIC ANHYDRASE II REVEALS THE ARCHITECTURE OF A REGULATORY CYSTEINE SWITCH1eou: CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH AN ANTICONVULSANT SUGAR SULFAMATE1f2w: THE MECHANISM OF CYANAMIDE HYDRATION CATALYZED BY CARBONIC ANHYDRASE II REVEALED BY CRYOGENIC X-RAY DIFFRACTION1fql: X-RAY CRYSTAL STRUCTURE OF ZINC-BOUND F95M/W97V CARBONIC ANHYDRASE (CAII) VARIANT1fqm: X-RAY CRYSTAL STRUCTURE OF ZINC-BOUND F93I/F95M/W97V CARBONIC ANHYDRASE (CAII) VARIANT1fqn: X-RAY CRYSTAL STRUCTURE OF METAL-FREE F93I/F95M/W97V CARBONIC ANHYDRASE (CAII) VARIANT1fqr: X-RAY CRYSTAL STRUCTURE OF COBALT-BOUND F93I/F95M/W97V CARBONIC ANHYDRASE (CAII) VARIANT1fr4: X-RAY CRYSTAL STRUCTURE OF COPPER-BOUND F93I/F95M/W97V CARBONIC ANHYDRASE (CAII) VARIANT1fr7: X-RAY CRYSTAL STRUCTURE OF ZINC-BOUND F93S/F95L/W97M CARBONIC ANHYDRASE (CAII) VARIANT1fsn: X-RAY CRYSTAL STRUCTURE OF METAL-FREE F93S/F95L/W97M CARBONIC ANHYDRASE (CAII) VARIANT1fsq: X-RAY CRYSTAL STRUCTURE OF COBALT-BOUND F93S/F95L/W97M CARBONIC ANHYDRASE (CAII) VARIANT1fsr: X-RAY CRYSTAL STRUCTURE OF COPPER-BOUND F93S/F95L/W97M CARBONIC ANHYDRASE (CAII) VARIANT1g0e: SITE-SPECIFIC MUTANT (HIS64 REPLACED WITH ALA) OF HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH 4-METHYLIMIDAZOLE1g0f: SITE-SPECIFIC MUTANT (HIS64 REPLACED WITH ALA) OF HUMAN CARBONIC ANHYDRASE II1g1d: CARBONIC ANHYDRASE II COMPLEXED WITH 4-(AMINOSULFONYL)-N--BENZAMIDE1g3z: CARBONIC ANHYDRASE II (F131V)1g45: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N--BENZAMIDE1g46: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N--BENZAMIDE1g48: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N--BENZAMIDE1g4j: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N--BENZAMIDE1g4o: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-PHENYLMETHYLBENZAMIDE1g52: CARBONIC ANHYDRASE II COMPLEXED WITH 4-(AMINOSULFONYL)-N--BENZAMIDE1g53: CARBONIC ANHYDRASE II COMPLEXED WITH 4-(AMINOSULFONYL)-N--BENZAMIDE1g54: CARBONIC ANHYDRASE II COMPLEXED WITH 4-(AMINOSULFONYL)-N--BENZAMIDE1g6v: Complex of the camelid heavy-chain antibody fragment CAB-CA05 with bovine carbonic anhydrase1h4n: H94N CARBONIC ANHYDRASE II COMPLEXED WITH TRIS1h9n: H119N CARBONIC ANHYDRASE II1h9q: H119Q CARBONIC ANHYDRASE II1hca: 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 II1hec: STRUCTURAL CONSEQUENCES OF HYDROPHILIC AMINO-ACID SUBSTITUTIONS IN THE HYDROPHOBIC POCKET OF HUMAN CARBONIC ANHYDRASE II1hed: STRUCTURAL CONSEQUENCES OF HYDROPHILIC AMINO-ACID SUBSTITUTIONS IN THE HYDROPHOBIC POCKET OF HUMAN CARBONIC ANHYDRASE II1hva: ENGINEERING THE ZINC BINDING SITE OF HUMAN CARBONIC ANHYDRASE II: STRUCTURE OF THE HIS-94-> CYS APOENZYME IN A NEW CRYSTALLINE FORM1i8z: CARBONIC ANHYDRASE II COMPLEXED WITH AL-6629 2H-THIENO-1,2-THIAZINE-6-SULFONAMIDE, 2-(3-METHOXYPHENYL)-3-(4-MORPHOLINYL)-, 1,1-DIOXIDE1i90: CARBONIC ANHYDRASE II COMPLEXED WITH AL-8520 2H-THIENO-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-1,2-THIAZINE-6-SULFONAMIDE, 2-(3-HYDROXYPHENYL)-3-(4-MORPHOLINYL)-, 1,1-DIOXIDE1i9l: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N--BENZAMIDE1i9m: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N--BENZAMIDE1i9n: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N--BENZAMIDE1i9o: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N--BENZAMIDE1i9p: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N--BENZAMIDE1i9q: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N--BENZAMIDE1if4: Carbonic Anhydrase II Complexed With 4-fluorobenzenesulfonamide1if5: Carbonic Anhydrase II Complexed With 2,6-difluorobenzenesulfonamide1if6: Carbonic Anhydrase II Complexed With 3,5-difluorobenzenesulfonamide1if7: Carbonic Anhydrase II Complexed With (R)-N-(3-Indol-1-yl-2-methyl-propyl)-4-sulfamoyl-benzamide1if8: Carbonic Anhydrase II Complexed With (S)-N-(3-Indol-1-yl-2-methyl-propyl)-4-sulfamoyl-benzamide1if9: Carbonic Anhydrase II Complexed With N--4-sulfamoyl-benzamide1kwq: HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH INHIBITOR 2000-071kwr: HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH INHIBITOR 0134-361lg5: Crystal Structure Analysis of the HCA II Mutant T199P in complex with beta-mercaptoethanol1lg6: Crystal Structure Analysis of HCA II Mutant T199P in Complex with Thiocyanate1lgd: Crystal Structure Analysis of HCA II Mutant T199P in Complex with Bicarbonate1lug: Full Matrix Error Analysis of Carbonic Anhydrase1lzv: Site-Specific Mutant (Tyr7 replaced with His) of Human Carbonic Anhydrase II1moo: Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at high resolution1mua: STRUCTURE AND ENERGETICS OF A NON-PROLINE CIS-PEPTIDYL LINKAGE IN AN ENGINEERED PROTEIN1okl: CARBONIC ANHYDRASE II COMPLEX WITH THE 1OKL INHIBITOR 5-DIMETHYLAMINO-NAPHTHALENE-1-SULFONAMIDE1okm: CARBONIC ANHYDRASE II COMPLEX WITH THE 1OKM INHIBITOR 4-SULFONAMIDE-BENZAMIDE1okn: CARBONIC ANHYDRASE II COMPLEX WITH THE 1OKN INHIBITOR 4-SULFONAMIDE-1oq5: CARBONIC ANHYDRASE II IN COMPLEX WITH NANOMOLAR INHIBITOR1ray: THE STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH BROMIDE AND AZIDE1raz: THE STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH BROMIDE AND AZIDE1rza: X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES1rzb: X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES1rzc: X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES1rzd: X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES1rze: X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES1t9n: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II1tb0: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II1tbt: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II1te3: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II1teq: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II1teu: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II1tg3: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II1tg9: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II1th9: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II1thk: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II1ttm: Human carbonic anhydrase II complexed with 667-coumate1uga: HUMAN CARBONIC ANHYDRASE II (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY PHE (A65F)1ugb: HUMAN CARBONIC ANHYDRASE II (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY GLY (A65G)1ugc: HUMAN CARBONIC ANHYDRASE II (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY HIS (A65H)1ugd: HUMAN CARBONIC ANHYDRASE II (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY SER (A65S)1uge: HUMAN CARBONIC ANHYDRASE II (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY LEU (A65L)1ugf: HUMAN CARBONIC ANHYDRASE II (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY THR (A65T)1ugg: HUMAN CARBONIC ANHYDRASE II (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY SER (A65S)-ORTHORHOMBIC FORM1xeg: Crystal structure of human carbonic anhydrase II complexed with an acetate ion1xev: Crystal structure of human carbonic anhydrase II in a new crystal form1xpz: Structure of human carbonic anhydrase II with 4--4H--triazole1xq0: Structure of human carbonic anhydrase II with 4--4H--triazole1yda: STRUCTURAL BASIS OF INHIBITOR AFFINITY TO VARIANTS OF HUMAN CARBONIC ANHYDRASE II1ydb: STRUCTURAL BASIS OF INHIBITOR AFFINITY TO VARIANTS OF HUMAN CARBONIC ANHYDRASE II1ydc: STRUCTURAL BASIS OF INHIBITOR AFFINITY TO VARIANTS OF HUMAN CARBONIC ANHYDRASE II1ydd: STRUCTURAL BASIS OF INHIBITOR AFFINITY TO VARIANTS OF HUMAN CARBONIC ANHYDRASE II1yo0: Proton Transfer from His200 in Human Carbonic Anhydrase II1yo1: Proton Transfer from His200 in Human Carbonic Anhydrase II1yo2: Proton Transfer from His200 in Human Carbonic Anhydrase II1z9y: carbonic anhydrase II in complex with furosemide as sulfonamide inhibitor1ze8: Carbonic anhydrase II in complex with a membrane-impermeant sulfonamide inhibitor1zfk: carbonic anhydrase II in complex with N-4-sulfonamidphenyl-N'-4-methylbenzosulfonylurease as sulfonamide inhibitor1zfq: carbonic anhydrase II in complex with ethoxzolamidphenole as sulfonamide inhibitor1zge: carbonic anhydrase II in complex with p-Sulfonamido-o,o'-dichloroaniline as sulfonamide inhibitor1zgf: carbonic anhydrase II in complex with trichloromethiazide as sulfonamide inhibitor1zh9: carbonic anhydrase II in complex with N-4-Methyl-1-piperazinyl-N'-(p-sulfonamide)phenylthiourea as sulfonamide inhibitor1zsa: CARBONIC ANHYDRASE II MUTANT E117Q, APO FORM1zsb: CARBONIC ANHYDRASE II MUTANT E117Q, TRANSITION STATE ANALOGUE ACETAZOLAMIDE1zsc: CARBONIC ANHYDRASE II MUTANT E117Q, HOLO FORM2abe: 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 activators2aw1: 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 Celecoxib2ax2: Production and X-ray crystallographic analysis of fully deuterated human carbonic anhydrase II2ca2: CRYSTALLOGRAPHIC STUDIES OF INHIBITOR BINDING SITES IN HUMAN CARBONIC ANHYDRASE II. A PENTACOORDINATED BINDING OF THE SCN-ION TO THE ZINC AT HIGH P*H2cba: STRUCTURE OF NATIVE AND APO CARBONIC ANHYDRASE II AND SOME OF ITS ANION-LIGAND COMPLEXES2cbb: STRUCTURE OF NATIVE AND APO CARBONIC ANHYDRASE II AND SOME OF ITS ANION-LIGAND COMPLEXES2cbc: STRUCTURE OF NATIVE AND APO CARBONIC ANHYDRASE II AND SOME OF ITS ANION-LIGAND COMPLEXES2cbd: STRUCTURE OF NATIVE AND APO CARBONIC ANHYDRASE II AND SOME OF ITS ANION-LIGAND COMPLEXES2cbe: STRUCTURE OF NATIVE AND APO CARBONIC ANHYDRASE II AND SOME OF ITS ANION-LIGAND COMPLEXES2eu2: Human Carbonic Anhydrase II in complex with novel inhibitors2eu3: Human Carbonic anhydrase II in complex with novel inhibitors2ez7: 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 enzyme2f14: The Crystal Structure of the Human Carbonic Anhydrase II in Complex with a Fluorescent Inhibitor2fmg: 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-phenylalanine2fmz: 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 donors2fnm: Activation of human carbonic anhdyrase II by exogenous proton donors2fnn: Activation of human carbonic anhydrase II by exogenous proton donors2foq: Human Carbonic Anhydrase II complexed with two-prong inhibitors2fos: Human Carbonic Anhydrase II complexed with two-prong inhibitors2fou: Human Carbonic Anhydrase II complexed with two-prong inhibitors2fov: Human Carbonic Anhydrase II complexed with two-prong inhibitors2gd8: Crystal structure analysis of the human carbonic anhydrase II in complex with a 2-substituted estradiol bis-sulfamate2geh: N-Hydroxyurea, a versatile zinc binding function in the design of metalloenzyme inhibitors2h15: Carbonic anhydrase inhibitors: Clashing with Ala65 as a means of designing isozyme-selective inhibitors that show low affinity for the ubiquitous isozyme II2h4n: H94N CARBONIC ANHYDRASE II COMPLEXED WITH ACETAZOLAMIDE2hd6: 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 isoforms2hl4: Crystal structure analysis of human carbonic anhydrase II in complex with a benzenesulfonamide derivative2hnc: 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 inhibitor2ili: Refine atomic structure of human carbonic anhydrase II2nng: Structure of inhibitor binding to Carbonic Anhydrase II2nno: Structure of inhibitor binding to Carbonic Anhydrase II2nns: Structure of inhibitor binding to Carbonic Anhydrase II2nnv: Structure of inhibitor binding to Carbonic Anhydrase II2nwo: Structural and kinetic effect of hydrophobic mutations in the active site of human carbonic anhydrase II2nwp: Structural and kinetic effects of hydrophobic mutations in the active site of human carbonic anhydrase II2nwy: Structural and kinetic effects of hydrophobic mutations on the active site of human carbonic anhydrase II2nwz: Structural and kinetic effects of hydrophobic mutations on the active site of human carbonic anhydrase II2nxr: Structural effects of hydrophobic mutations on the active site of human carbonic anhydrase II2nxs: Structural and kinetic effects of hydrophobic mutations in the active site of human carbonic anhydrase II2nxt: Structural and kinetic effects of hydrophobic mutations in the active site of human carbonic anhydrase II2o4z: Crystal structure of the Carbonic Anhydrase II complexed with hydroxysulfamide inhibitor3ca2: CRYSTALLOGRAPHIC STUDIES OF INHIBITOR BINDING SITES IN HUMAN CARBONIC ANHYDRASE II. A PENTACOORDINATED BINDING OF THE SCN-ION TO THE ZINC AT HIGH P*H4ca2: ENGINEERING THE HYDROPHOBIC POCKET OF CARBONIC ANHYDRASE II4cac: REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE II AT 2.0 ANGSTROMS RESOLUTION5ca2: CONFORMATIONAL MOBILITY OF HIS-64 IN THE THR-200 (RIGHT ARROW) SER MUTANT OF HUMAN CARBONIC ANHYDRASE II5cac: REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE II AT 2.0 ANGSTROMS RESOLUTION6ca2: ENGINEERING THE HYDROPHOBIC POCKET OF CARBONIC ANHYDRASE II7ca2: ENGINEERING THE HYDROPHOBIC POCKET OF CARBONIC ANHYDRASE II8ca2: ENGINEERING THE HYDROPHOBIC POCKET OF CARBONIC ANHYDRASE II9ca2: ENGINEERING THE HYDROPHOBIC POCKET OF CARBONIC ANHYDRASE II Carbonic anhydrase II (gene name CA2), is one of sixteen forms of human α carbonic anhydrases . 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. Loss of carbonic anhydrase activity in bones impairs the ability of osteoclasts to promote bone resorption, leading to osteopetrosis. Carbonic anhydrase II has been shown to interact with band 3 and sodium-hydrogen antiporter 1.