eF-site ID 1gsf-C PDB Code 1gsf Chain C click to enlarge Title GLUTATHIONE TRANSFERASE A1-1 COMPLEXED WITH ETHACRYNIC ACID Classification TRANSFERASE (GLUTATHIONE) Compound GLUTATHIONE TRANSFERASE A1-1 Source Homo sapiens (Human) (GSTA1_HUMAN) Sequence C:  AEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDL DKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNL YGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAKL ALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLV ELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPG SPRKPPMDEKSLEEARKIFRF Description Functional site 1) chain C residue 9 type sequence Y description BINDING SITE FOR RESIDUE EAA C 223 source : AC3 2) chain C residue 10 type sequence F description BINDING SITE FOR RESIDUE EAA C 223 source : AC3 3) chain C residue 14 type sequence G description BINDING SITE FOR RESIDUE EAA C 223 source : AC3 4) chain C residue 15 type sequence R description BINDING SITE FOR RESIDUE EAA C 223 source : AC3 5) chain C residue 55 type sequence V description BINDING SITE FOR RESIDUE EAA C 223 source : AC3 6) chain C residue 107 type sequence L description BINDING SITE FOR RESIDUE EAA C 223 source : AC3 7) chain C residue 111 type sequence V description BINDING SITE FOR RESIDUE EAA C 223 source : AC3 8) chain C residue 208 type sequence M description BINDING SITE FOR RESIDUE EAA C 223 source : AC3 9) chain C residue 220 type sequence F description BINDING SITE FOR RESIDUE EAA C 223 source : AC3 10) chain C residue 46 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965 source Swiss-Prot : SWS_FT_FI1 11) chain C residue 55 type BINDING sequence V description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965 source Swiss-Prot : SWS_FT_FI1 12) chain C residue 68 type BINDING sequence T description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965 source Swiss-Prot : SWS_FT_FI1 13) chain C residue 10 type BINDING sequence F description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965 source Swiss-Prot : SWS_FT_FI1 14) chain C residue 2 type MOD_RES sequence A description N-acetylmethionine => ECO:0000250|UniProtKB:P80894 source Swiss-Prot : SWS_FT_FI2 15) chain C 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 16) chain C residue 5 type MOD_RES sequence P description N6-succinyllysine => ECO:0000250|UniProtKB:P30115 source Swiss-Prot : SWS_FT_FI4

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