eF-site ID 1qrf-A PDB Code 1qrf Chain A click to enlarge Title A CLOSER LOOK AT THE ACTIVE SITE OF GAMMA-CARBONIC ANHYDRASES: HIGH RESOLUTION CRYSTALLOGRAPHIC STUDIES OF THE CARBONIC ANHYDRASE FROM METHANOSARCINA THERMOPHILA Classification LYASE Compound CARBONIC ANHYDRASE Source Methanosarcina thermophila (CAH_METTE) Sequence A:  FSNIRENPVTPWNPEPSAPVIDPTAYIDPQASVIGEVTIG ANVMVSPMASIRSDEGMPIFVGDRSNVQDGVVLHALETIN EEGEPIEDNIVEVDGKEYAVYIGNNVSLAHQSQVHGPAAV GDDTFIGMQAFVFKSKVGNNCVLEPRSAAIGVTIPDGRYI PAGMVVTSQAEADKLPEVTDDYAYSHTNEAVVYVNVHLAE GYKETS Description Functional site 1) chain A residue 62 type sequence E description BINDING SITE FOR RESIDUE SO4 A 215 source : AC1 2) chain A residue 75 type sequence Q description BINDING SITE FOR RESIDUE SO4 A 215 source : AC1 3) chain A residue 81 type sequence H description BINDING SITE FOR RESIDUE SO4 A 215 source : AC1 4) chain A residue 122 type sequence H description BINDING SITE FOR RESIDUE SO4 A 215 source : AC1 5) chain A residue 198 type sequence V description BINDING SITE FOR RESIDUE SO4 A 215 source : AC1 6) chain A residue 202 type sequence N description BINDING SITE FOR RESIDUE SO4 A 215 source : AC1 7) chain A residue 81 type sequence H description BINDING SITE FOR RESIDUE CO A 214 source : AC2 8) chain A residue 117 type sequence H description BINDING SITE FOR RESIDUE CO A 214 source : AC2 9) chain A residue 122 type sequence H description BINDING SITE FOR RESIDUE CO A 214 source : AC2 10) chain A residue 62 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000305|PubMed:10924115 source Swiss-Prot : SWS_FT_FI1 11) chain A residue 84 type ACT_SITE sequence E description ACT_SITE => ECO:0000305|PubMed:10924115 source Swiss-Prot : SWS_FT_FI2 12) chain A residue 62 type catalytic sequence E description 516 source MCSA : MCSA1 13) chain A residue 75 type catalytic sequence Q description 516 source MCSA : MCSA1 14) chain A residue 81 type catalytic sequence H description 516 source MCSA : MCSA1 15) chain A residue 84 type catalytic sequence E description 516 source MCSA : MCSA1 16) chain A residue 117 type catalytic sequence H description 516 source MCSA : MCSA1 17) chain A residue 122 type catalytic sequence H description 516 source MCSA : MCSA1 18) chain A residue 202 type catalytic sequence N description 516 source MCSA : MCSA1 19) chain A residue 59 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10924115 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 75 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10924115 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 202 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10924115 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 81 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10924115, ECO:0000269|PubMed:8665839, ECO:0007744|PDB:1QRG, ECO:0007744|PDB:1QRL, ECO:0007744|PDB:1QRM, ECO:0007744|PDB:1THJ source Swiss-Prot : SWS_FT_FI4 23) chain A residue 117 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10924115, ECO:0000269|PubMed:8665839, ECO:0007744|PDB:1QRG, ECO:0007744|PDB:1QRL, ECO:0007744|PDB:1QRM, ECO:0007744|PDB:1THJ source Swiss-Prot : SWS_FT_FI4 24) chain A residue 122 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10924115, ECO:0000269|PubMed:8665839, ECO:0007744|PDB:1QRG, ECO:0007744|PDB:1QRL, ECO:0007744|PDB:1QRM, ECO:0007744|PDB:1THJ source Swiss-Prot : SWS_FT_FI4

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