eF-site ID 1pgt-A PDB Code 1pgt Chain A click to enlarge Title CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE S-TRANSFERASE P1-1[V104] COMPLEXED WITH S-HEXYLGLUTATHIONE Classification TRANSFERASE Compound GLUTATHIONE S-TRANSFERASE Source Homo sapiens (Human) (GSTP1_HUMAN) Sequence A:  MPPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQ EGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLY GKDQQEAALVDMVNDGVEDLRCKYVSLIYTNYEAGKDDYV KALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLL LIHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYV NLPINGNGKQ Description Functional site 1) chain A residue 7 type sequence Y description BINDING SITE FOR RESIDUE GTX A 210 source : AC1 2) chain A residue 8 type sequence F description BINDING SITE FOR RESIDUE GTX A 210 source : AC1 3) chain A residue 13 type sequence R description BINDING SITE FOR RESIDUE GTX A 210 source : AC1 4) chain A residue 35 type sequence V description BINDING SITE FOR RESIDUE GTX A 210 source : AC1 5) chain A residue 38 type sequence W description BINDING SITE FOR RESIDUE GTX A 210 source : AC1 6) chain A residue 44 type sequence K description BINDING SITE FOR RESIDUE GTX A 210 source : AC1 7) chain A residue 51 type sequence Q description BINDING SITE FOR RESIDUE GTX A 210 source : AC1 8) chain A residue 52 type sequence L description BINDING SITE FOR RESIDUE GTX A 210 source : AC1 9) chain A residue 53 type sequence P description BINDING SITE FOR RESIDUE GTX A 210 source : AC1 10) chain A residue 64 type sequence Q description BINDING SITE FOR RESIDUE GTX A 210 source : AC1 11) chain A residue 65 type sequence S description BINDING SITE FOR RESIDUE GTX A 210 source : AC1 12) chain A residue 108 type sequence Y description BINDING SITE FOR RESIDUE GTX A 210 source : AC1 13) chain A residue 22 type sequence A description BINDING SITE FOR RESIDUE EPE A 211 source : AC2 14) chain A residue 28 type sequence W description BINDING SITE FOR RESIDUE EPE A 211 source : AC2 15) chain A residue 29 type sequence K description BINDING SITE FOR RESIDUE EPE A 211 source : AC2 16) chain A residue 30 type sequence E description BINDING SITE FOR RESIDUE EPE A 211 source : AC2 17) chain A residue 197 type sequence E description BINDING SITE FOR RESIDUE EPE A 211 source : AC2 18) chain A residue 98 type sequence D description BINDING SITE FOR RESIDUE GTX B 210 source : AC3 19) chain A residue 171 type sequence D description BINDING SITE FOR RESIDUE EPE B 211 source : AC4 20) chain A residue 7 type catalytic sequence Y description 993 source MCSA : MCSA1 21) chain A residue 7 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 13 type BINDING sequence R description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 38 type BINDING sequence W description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 44 type BINDING sequence K description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 51 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 64 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 3 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 198 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 61 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 102 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P19157 source Swiss-Prot : SWS_FT_FI4 31) chain A residue 115 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P19157 source Swiss-Prot : SWS_FT_FI4 32) chain A residue 127 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI5

Display surface Download Links