eF-site ID 1azm-A PDB Code 1azm Chain A click to enlarge Title DRUG-PROTEIN INTERACTIONS: STRUCTURE OF SULFONAMIDE DRUG COMPLEXED WITH HUMAN CARBONIC ANHYDRASE I Classification LYASE(OXO-ACID) Compound CARBONIC ANHYDRASE I Source Homo sapiens (Human) (CAH1_HUMAN) Sequence A:  PDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDT SLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVLKGG PFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAH WNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVLD ALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPP LYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVPMQ HNNRPTQPLKGRTVRASF Description Functional site 1) chain A residue 7 type sequence Y description CATALYTIC SITE source : CAT 2) chain A residue 62 type sequence V description CATALYTIC SITE source : CAT 3) chain A residue 64 type sequence H description CATALYTIC SITE source : CAT 4) chain A residue 65 type sequence S description CATALYTIC SITE source : CAT 5) chain A residue 67 type sequence H description CATALYTIC SITE source : CAT 6) chain A residue 69 type sequence N description CATALYTIC SITE source : CAT 7) chain A residue 92 type sequence Q description CATALYTIC SITE source : CAT 8) chain A residue 106 type sequence E description CATALYTIC SITE source : CAT 9) chain A residue 117 type sequence E description CATALYTIC SITE source : CAT 10) chain A residue 199 type sequence T description CATALYTIC SITE source : CAT 11) chain A residue 200 type sequence H description CATALYTIC SITE source : CAT 12) chain A residue 91 type sequence F description CATALYTIC SITE source : CAT 13) chain A residue 121 type sequence A description CATALYTIC SITE source : CAT 14) chain A residue 131 type sequence L description CATALYTIC SITE source : CAT 15) chain A residue 135 type sequence A description CATALYTIC SITE source : CAT 16) chain A residue 141 type sequence L description CATALYTIC SITE source : CAT 17) chain A residue 143 type sequence V description CATALYTIC SITE source : CAT 18) chain A residue 198 type sequence L description CATALYTIC SITE source : CAT 19) chain A residue 201 type sequence P description CATALYTIC SITE source : CAT 20) chain A residue 202 type sequence P description CATALYTIC SITE source : CAT 21) chain A residue 204 type sequence Y description CATALYTIC SITE source : CAT 22) chain A residue 206 type sequence S description CATALYTIC SITE source : CAT 23) chain A residue 207 type sequence V description CATALYTIC SITE source : CAT 24) chain A residue 209 type sequence W description CATALYTIC SITE source : CAT 25) chain A residue 94 type sequence H description BINDING SITE FOR RESIDUE ZN A 261 source : AC1 26) chain A residue 96 type sequence H description BINDING SITE FOR RESIDUE ZN A 261 source : AC1 27) chain A residue 119 type sequence H description BINDING SITE FOR RESIDUE ZN A 261 source : AC1 28) chain A residue 91 type sequence F description BINDING SITE FOR RESIDUE AZM A 262 source : AC2 29) chain A residue 94 type sequence H description BINDING SITE FOR RESIDUE AZM A 262 source : AC2 30) chain A residue 96 type sequence H description BINDING SITE FOR RESIDUE AZM A 262 source : AC2 31) chain A residue 119 type sequence H description BINDING SITE FOR RESIDUE AZM A 262 source : AC2 32) chain A residue 198 type sequence L description BINDING SITE FOR RESIDUE AZM A 262 source : AC2 33) chain A residue 199 type sequence T description BINDING SITE FOR RESIDUE AZM A 262 source : AC2 34) chain A residue 200 type sequence H description BINDING SITE FOR RESIDUE AZM A 262 source : AC2 35) chain A residue 209 type sequence W description BINDING SITE FOR RESIDUE AZM A 262 source : AC2 36) chain A residue 65 type ACT_SITE sequence S description Proton donor/acceptor => ECO:0000250|UniProtKB:P00918 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 65 type BINDING sequence S description in variant Michigan-1 => ECO:0000269|PubMed:12009884 source Swiss-Prot : SWS_FT_FI2 38) chain A residue 68 type BINDING sequence V description in variant Michigan-1 => ECO:0000269|PubMed:12009884 source Swiss-Prot : SWS_FT_FI2 39) chain A residue 201 type BINDING sequence P description in variant Michigan-1 => ECO:0000269|PubMed:12009884 source Swiss-Prot : SWS_FT_FI2 40) chain A residue 95 type BINDING sequence F description BINDING => ECO:0000269|PubMed:12009884, ECO:0000269|PubMed:15299369, ECO:0000269|PubMed:16506782, ECO:0000269|PubMed:16870440, ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17407288, ECO:0000269|PubMed:6430186, ECO:0000269|PubMed:7932756, ECO:0000269|PubMed:804171, ECO:0000269|PubMed:8057362 source Swiss-Prot : SWS_FT_FI3 41) chain A residue 97 type BINDING sequence W description BINDING => ECO:0000269|PubMed:12009884, ECO:0000269|PubMed:15299369, ECO:0000269|PubMed:16506782, ECO:0000269|PubMed:16870440, ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17407288, ECO:0000269|PubMed:6430186, ECO:0000269|PubMed:7932756, ECO:0000269|PubMed:804171, ECO:0000269|PubMed:8057362 source Swiss-Prot : SWS_FT_FI3 42) chain A residue 120 type BINDING sequence V description BINDING => ECO:0000269|PubMed:12009884, ECO:0000269|PubMed:15299369, ECO:0000269|PubMed:16506782, ECO:0000269|PubMed:16870440, ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17407288, ECO:0000269|PubMed:6430186, ECO:0000269|PubMed:7932756, ECO:0000269|PubMed:804171, ECO:0000269|PubMed:8057362 source Swiss-Prot : SWS_FT_FI3 43) chain A residue 200 type BINDING sequence H description BINDING => ECO:0000269|PubMed:8057362 source Swiss-Prot : SWS_FT_FI4 44) chain A residue 105-121 type prosite sequence SEHTVDGVKYSAELHVA description ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdgvkYsaELHVA source prosite : PS00162

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