eF-site ID 1gse-A PDB Code 1gse Chain A click to enlarge Title GLUTATHIONE TRANSFERASE A1-1 COMPLEXED WITH AN ETHACRYNIC ACID GLUTATHIONE CONJUGATE (MUTANT R15K) Classification TRANSFERASE (GLUTATHIONE) Compound GLUTATHIONE TRANSFERASE Source Homo sapiens (Human) (GTA1_HUMAN) Sequence A:  AEKPKLHYFNARGKMESTRWLLAAAGVEFEEKFIKSAEDL DKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNL YGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAKL ALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLV ELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPG SPRKPPMDEKSLEEARKIFRF Description Functional site 1) chain A residue 9 type sequence Y description BINDING SITE FOR RESIDUE GSH A 223 source : AC1 2) chain A residue 45 type sequence R description BINDING SITE FOR RESIDUE GSH A 223 source : AC1 3) chain A residue 54 type sequence Q description BINDING SITE FOR RESIDUE GSH A 223 source : AC1 4) chain A residue 55 type sequence V description BINDING SITE FOR RESIDUE GSH A 223 source : AC1 5) chain A residue 56 type sequence P description BINDING SITE FOR RESIDUE GSH A 223 source : AC1 6) chain A residue 67 type sequence Q description BINDING SITE FOR RESIDUE GSH A 223 source : AC1 7) chain A residue 68 type sequence T description BINDING SITE FOR RESIDUE GSH A 223 source : AC1 8) chain A residue 9 type sequence Y description BINDING SITE FOR RESIDUE EAA A 224 source : AC2 9) chain A residue 10 type sequence F description BINDING SITE FOR RESIDUE EAA A 224 source : AC2 10) chain A residue 13 type sequence R description BINDING SITE FOR RESIDUE EAA A 224 source : AC2 11) chain A residue 14 type sequence G description BINDING SITE FOR RESIDUE EAA A 224 source : AC2 12) chain A residue 15 type sequence K description BINDING SITE FOR RESIDUE EAA A 224 source : AC2 13) chain A residue 107 type sequence L description BINDING SITE FOR RESIDUE EAA A 224 source : AC2 14) chain A residue 108 type sequence L description BINDING SITE FOR RESIDUE EAA A 224 source : AC2 15) chain A residue 111 type sequence V description BINDING SITE FOR RESIDUE EAA A 224 source : AC2 16) chain A residue 208 type sequence M description BINDING SITE FOR RESIDUE EAA A 224 source : AC2 17) chain A residue 216 type sequence A description BINDING SITE FOR RESIDUE EAA A 224 source : AC2 18) chain A residue 220 type sequence F description BINDING SITE FOR RESIDUE EAA A 224 source : AC2 19) chain A residue 222 type sequence F description BINDING SITE FOR RESIDUE EAA A 224 source : AC2 20) chain A residue 18 type sequence S description BINDING SITE FOR RESIDUE BME A 225 source : AC3 21) chain A residue 96 type sequence I description BINDING SITE FOR RESIDUE BME A 225 source : AC3 22) chain A residue 69 type sequence R description BINDING SITE FOR RESIDUE BME A 226 source : AC4 23) chain A residue 72 type sequence L description BINDING SITE FOR RESIDUE BME A 226 source : AC4 24) chain A residue 96 type sequence I description BINDING SITE FOR RESIDUE BME A 226 source : AC4 25) chain A residue 97 type sequence E description BINDING SITE FOR RESIDUE BME A 226 source : AC4 26) chain A residue 159 type sequence H description BINDING SITE FOR RESIDUE BME A 226 source : AC4 27) chain A residue 101 type sequence D description BINDING SITE FOR RESIDUE GSH B 223 source : AC5 28) chain A residue 131 type sequence R description BINDING SITE FOR RESIDUE GSH B 223 source : AC5 29) chain A residue 10 type BINDING sequence F description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 46 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 55 type BINDING sequence V description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 68 type BINDING sequence T description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 5 type MOD_RES sequence P description N6-succinyllysine => ECO:0000250|UniProtKB:P30115 source Swiss-Prot : SWS_FT_FI4 34) chain A residue 2 type MOD_RES sequence A description N-acetylmethionine => ECO:0000250|UniProtKB:P80894 source Swiss-Prot : SWS_FT_FI2 35) chain A residue 3 type MOD_RES sequence E description N-acetylalanine; in Glutathione S-transferase A1, N-terminally processed => ECO:0000250|UniProtKB:P30115 source Swiss-Prot : SWS_FT_FI3

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