eF-site ID 3pgt-A PDB Code 3pgt Chain A click to enlarge Title CRYSTAL STRUCTURE OF HGSTP1-1[I104] COMPLEXED WITH THE GSH CONJUGATE OF (+)-ANTI-BPDE Classification TRANSFERASE Compound PROTEIN (GLUTATHIONE S-TRANSFERASE) Source (GSTP1_HUMAN) Sequence A:  MPPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQ EGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLY GKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYV KALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLL LIHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYV NLPINGNGKQ Description Functional site 1) chain A residue 51 type sequence Q description BINDING SITE FOR RESIDUE SO4 A 210 source : AC2 2) chain A residue 105 type sequence S description BINDING SITE FOR RESIDUE SO4 A 211 source : AC4 3) chain A residue 74 type sequence R description BINDING SITE FOR RESIDUE SO4 A 212 source : AC5 4) chain A residue 79 type sequence Y description BINDING SITE FOR RESIDUE SO4 A 212 source : AC5 5) chain A residue 190 type sequence K description BINDING SITE FOR RESIDUE SO4 A 213 source : AC6 6) chain A residue 8 type sequence F description BINDING SITE FOR RESIDUE GBX A 214 source : AC8 7) chain A residue 10 type sequence V description BINDING SITE FOR RESIDUE GBX A 214 source : AC8 8) chain A residue 13 type sequence R description BINDING SITE FOR RESIDUE GBX A 214 source : AC8 9) chain A residue 38 type sequence W description BINDING SITE FOR RESIDUE GBX A 214 source : AC8 10) chain A residue 44 type sequence K description BINDING SITE FOR RESIDUE GBX A 214 source : AC8 11) chain A residue 51 type sequence Q description BINDING SITE FOR RESIDUE GBX A 214 source : AC8 12) chain A residue 52 type sequence L description BINDING SITE FOR RESIDUE GBX A 214 source : AC8 13) chain A residue 53 type sequence P description BINDING SITE FOR RESIDUE GBX A 214 source : AC8 14) chain A residue 64 type sequence Q description BINDING SITE FOR RESIDUE GBX A 214 source : AC8 15) chain A residue 65 type sequence S description BINDING SITE FOR RESIDUE GBX A 214 source : AC8 16) chain A residue 108 type sequence Y description BINDING SITE FOR RESIDUE GBX A 214 source : AC8 17) chain A residue 205 type sequence G description BINDING SITE FOR RESIDUE GBX A 214 source : AC8 18) chain A residue 22 type sequence A description BINDING SITE FOR RESIDUE MES A 215 source : AC9 19) chain A residue 28 type sequence W description BINDING SITE FOR RESIDUE MES A 215 source : AC9 20) chain A residue 30 type sequence E description BINDING SITE FOR RESIDUE MES A 215 source : AC9 21) chain A residue 197 type sequence E description BINDING SITE FOR RESIDUE MES A 215 source : AC9 22) chain A residue 8 type sequence F description BINDING SITE FOR RESIDUE MES A 216 source : BC1 23) chain A residue 35 type sequence V description BINDING SITE FOR RESIDUE MES A 216 source : BC1 24) chain A residue 38 type sequence W description BINDING SITE FOR RESIDUE MES A 216 source : BC1 25) chain A residue 98 type sequence D description BINDING SITE FOR RESIDUE GBX B 213 source : BC2 26) 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 27) 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 28) 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 29) 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 30) 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 31) 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 32) chain A residue 3 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954 source Swiss-Prot : SWS_FT_FI2 33) chain A residue 198 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954 source Swiss-Prot : SWS_FT_FI2 34) chain A residue 61 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 35) chain A residue 102 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P19157 source Swiss-Prot : SWS_FT_FI4 36) chain A residue 115 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P19157 source Swiss-Prot : SWS_FT_FI4 37) chain A residue 127 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI5

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