eF-site ID 16gs-A PDB Code 16gs Chain A click to enlarge Title GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 3 Classification TRANSFERASE Compound GLUTATHIONE S-TRANSFERASE Source null (GSTP1_HUMAN) Sequence A:  PYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEG SLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGK DQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKA LPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLI HEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNL PINGNGKQ Description Functional site 1) chain A residue 66 type sequence N description BINDING SITE FOR RESIDUE SO4 A 210 source : AC1 2) chain A residue 70 type sequence R description BINDING SITE FOR RESIDUE SO4 A 210 source : AC1 3) chain A residue 94 type sequence D description BINDING SITE FOR RESIDUE SO4 A 210 source : AC1 4) chain A residue 97 type sequence E description BINDING SITE FOR RESIDUE SO4 A 210 source : AC1 5) chain A residue 22 type sequence A description BINDING SITE FOR RESIDUE MES A 211 source : AC2 6) chain A residue 28 type sequence W description BINDING SITE FOR RESIDUE MES A 211 source : AC2 7) chain A residue 30 type sequence E description BINDING SITE FOR RESIDUE MES A 211 source : AC2 8) chain A residue 197 type sequence E description BINDING SITE FOR RESIDUE MES A 211 source : AC2 9) chain A residue 171 type sequence D description BINDING SITE FOR RESIDUE MES B 210 source : AC3 10) 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 11) 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 12) 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 13) 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 14) 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 15) 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 16) chain A residue 3 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 198 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 61 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 102 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P19157 source Swiss-Prot : SWS_FT_FI4 20) chain A residue 115 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P19157 source Swiss-Prot : SWS_FT_FI4 21) 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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