eF-site ID 3pgt-B PDB Code 3pgt Chain B 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 B:  PPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQE GSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYG KDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVK ALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLL IHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVN LPINGNGKQ Description Functional site 1) chain B residue 142 type sequence F description BINDING SITE FOR RESIDUE SO4 B 210 source : AC1 2) chain B residue 186 type sequence R description BINDING SITE FOR RESIDUE SO4 B 210 source : AC1 3) chain B residue 102 type sequence K description BINDING SITE FOR RESIDUE SO4 A 210 source : AC2 4) chain B residue 46 type sequence S description BINDING SITE FOR RESIDUE SO4 B 211 source : AC3 5) chain B residue 54 type sequence K description BINDING SITE FOR RESIDUE SO4 B 211 source : AC3 6) chain B residue 74 type sequence R description BINDING SITE FOR RESIDUE SO4 A 212 source : AC5 7) chain B residue 79 type sequence Y description BINDING SITE FOR RESIDUE SO4 A 212 source : AC5 8) chain B residue 115 type sequence K description BINDING SITE FOR RESIDUE SO4 B 212 source : AC7 9) chain B residue 98 type sequence D description BINDING SITE FOR RESIDUE GBX A 214 source : AC8 10) chain B residue 8 type sequence F description BINDING SITE FOR RESIDUE GBX B 213 source : BC2 11) chain B residue 10 type sequence V description BINDING SITE FOR RESIDUE GBX B 213 source : BC2 12) chain B residue 13 type sequence R description BINDING SITE FOR RESIDUE GBX B 213 source : BC2 13) chain B residue 38 type sequence W description BINDING SITE FOR RESIDUE GBX B 213 source : BC2 14) chain B residue 44 type sequence K description BINDING SITE FOR RESIDUE GBX B 213 source : BC2 15) chain B residue 50 type sequence G description BINDING SITE FOR RESIDUE GBX B 213 source : BC2 16) chain B residue 51 type sequence Q description BINDING SITE FOR RESIDUE GBX B 213 source : BC2 17) chain B residue 52 type sequence L description BINDING SITE FOR RESIDUE GBX B 213 source : BC2 18) chain B residue 53 type sequence P description BINDING SITE FOR RESIDUE GBX B 213 source : BC2 19) chain B residue 64 type sequence Q description BINDING SITE FOR RESIDUE GBX B 213 source : BC2 20) chain B residue 65 type sequence S description BINDING SITE FOR RESIDUE GBX B 213 source : BC2 21) chain B residue 108 type sequence Y description BINDING SITE FOR RESIDUE GBX B 213 source : BC2 22) chain B residue 205 type sequence G description BINDING SITE FOR RESIDUE GBX B 213 source : BC2 23) chain B residue 22 type sequence A description BINDING SITE FOR RESIDUE MES B 214 source : BC3 24) chain B residue 28 type sequence W description BINDING SITE FOR RESIDUE MES B 214 source : BC3 25) chain B residue 30 type sequence E description BINDING SITE FOR RESIDUE MES B 214 source : BC3 26) chain B residue 197 type sequence E description BINDING SITE FOR RESIDUE MES B 214 source : BC3 27) chain B residue 8 type sequence F description BINDING SITE FOR RESIDUE MES B 215 source : BC4 28) chain B residue 38 type sequence W description BINDING SITE FOR RESIDUE MES B 215 source : BC4 29) chain B 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 B 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 B 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 B 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 33) chain B 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 34) chain B 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 35) chain B residue 3 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954 source Swiss-Prot : SWS_FT_FI2 36) chain B residue 198 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954 source Swiss-Prot : SWS_FT_FI2 37) chain B residue 61 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 38) chain B residue 102 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P19157 source Swiss-Prot : SWS_FT_FI4 39) chain B residue 115 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P19157 source Swiss-Prot : SWS_FT_FI4 40) chain B residue 127 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI5

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