eF-site ID 16gs-B PDB Code 16gs Chain B click to enlarge Title GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 3 Classification TRANSFERASE Compound GLUTATHIONE S-TRANSFERASE Source null (GSTP1_HUMAN) Sequence B:  PYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEG SLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGK DQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKA LPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLI HEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNL PINGNGKQ Description Functional site 1) chain B residue 66 type sequence N description BINDING SITE FOR RESIDUE SO4 A 210 source : AC1 2) chain B residue 70 type sequence R description BINDING SITE FOR RESIDUE SO4 A 210 source : AC1 3) chain B residue 94 type sequence D description BINDING SITE FOR RESIDUE SO4 A 210 source : AC1 4) chain B residue 97 type sequence E description BINDING SITE FOR RESIDUE SO4 A 210 source : AC1 5) chain B residue 171 type sequence D description BINDING SITE FOR RESIDUE MES A 211 source : AC2 6) chain B residue 22 type sequence A description BINDING SITE FOR RESIDUE MES B 210 source : AC3 7) chain B residue 28 type sequence W description BINDING SITE FOR RESIDUE MES B 210 source : AC3 8) chain B residue 30 type sequence E description BINDING SITE FOR RESIDUE MES B 210 source : AC3 9) chain B residue 197 type sequence E description BINDING SITE FOR RESIDUE MES B 210 source : AC3 10) chain B residue 8 type BINDING sequence F 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 11) chain B residue 14 type BINDING sequence C 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 12) chain B residue 45 type BINDING sequence A 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 13) chain B residue 52 type BINDING sequence L 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 14) chain B residue 65 type BINDING sequence S 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 15) chain B residue 39 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 16) chain B residue 4 type MOD_RES sequence T description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954 source Swiss-Prot : SWS_FT_FI2 17) chain B residue 199 type MOD_RES sequence V description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 62 type MOD_RES sequence L description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 19) chain B residue 103 type MOD_RES sequence Y description N6-succinyllysine => ECO:0000250|UniProtKB:P19157 source Swiss-Prot : SWS_FT_FI4 20) chain B residue 116 type MOD_RES sequence D description N6-succinyllysine => ECO:0000250|UniProtKB:P19157 source Swiss-Prot : SWS_FT_FI4 21) chain B residue 128 type MOD_RES sequence P description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI5

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