eF-site ID 1pkz-AB PDB Code 1pkz Chain A, B click to enlarge Title Crystal structure of human glutathione transferase (GST) A1-1 Classification TRANSFERASE Compound Glutathione S-transferase A1 Source Homo sapiens (Human) (GSTA1_HUMAN) Sequence A:  AEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDL DKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNL YGKDIKERALIDMYIEGIADLGEMILLLPVXPPEEKDAKL ALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLV ELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPG SPRKPPMDEKSLEE B:  AEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDL DKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNL YGKDIKERALIDMYIEGIADLGEMILLLPVXPPEEKDAKL ALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLV ELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPG SPRKPPMDEKSLEEARKI Description (1)  Glutathione S-transferase A1 (E.C.2.5.1.18) Functional site 1) chain A residue 18 type sequence S description BINDING SITE FOR RESIDUE HED A 657 source : AC1 2) chain A residue 68 type sequence T description BINDING SITE FOR RESIDUE HED A 657 source : AC1 3) chain A residue 69 type sequence R description BINDING SITE FOR RESIDUE HED A 657 source : AC1 4) chain A residue 72 type sequence L description BINDING SITE FOR RESIDUE HED A 657 source : AC1 5) chain A residue 96 type sequence I description BINDING SITE FOR RESIDUE HED A 657 source : AC1 6) chain A residue 100 type sequence A description BINDING SITE FOR RESIDUE HED A 657 source : AC1 7) chain A residue 155 type sequence R description BINDING SITE FOR RESIDUE HED A 657 source : AC1 8) chain B residue 18 type sequence S description BINDING SITE FOR RESIDUE HED B 659 source : AC2 9) chain B residue 69 type sequence R description BINDING SITE FOR RESIDUE HED B 659 source : AC2 10) chain B residue 96 type sequence I description BINDING SITE FOR RESIDUE HED B 659 source : AC2 11) chain B residue 97 type sequence E description BINDING SITE FOR RESIDUE HED B 659 source : AC2 12) chain B residue 159 type sequence H description BINDING SITE FOR RESIDUE HED B 659 source : AC2 13) chain A residue 9 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 45 type BINDING sequence R description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 54 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 67 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965 source Swiss-Prot : SWS_FT_FI1 17) chain B residue 9 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965 source Swiss-Prot : SWS_FT_FI1 18) chain B residue 45 type BINDING sequence R description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965 source Swiss-Prot : SWS_FT_FI1 19) chain B residue 54 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 67 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 2 type MOD_RES sequence A description N-acetylalanine; in Glutathione S-transferase A1, N-terminally processed => ECO:0000250|UniProtKB:P30115 source Swiss-Prot : SWS_FT_FI3 22) chain B residue 2 type MOD_RES sequence A description N-acetylalanine; in Glutathione S-transferase A1, N-terminally processed => ECO:0000250|UniProtKB:P30115 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 4 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P30115 source Swiss-Prot : SWS_FT_FI4 24) chain B residue 4 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P30115 source Swiss-Prot : SWS_FT_FI4

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