eF-site ID 1zgn-A PDB Code 1zgn Chain A click to enlarge Title Crystal Structure of the Glutathione Transferase Pi in Complex with Dinitrosyl-diglutathionyl Iron Complex Classification TRANSFERASE Compound Glutathione S-transferase P Source Homo sapiens (Human) (GSTP1_HUMAN) Sequence A:  PYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEG SLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGK DQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKA LPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLI HEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNL PINGNGKQ Description Functional site 1) chain A residue 7 type sequence Y description BINDING SITE FOR RESIDUE FE A 1222 source : AC1 2) chain A residue 22 type sequence A description BINDING SITE FOR RESIDUE MES A 1220 source : AC3 3) chain A residue 26 type sequence Q description BINDING SITE FOR RESIDUE MES A 1220 source : AC3 4) chain A residue 28 type sequence W description BINDING SITE FOR RESIDUE MES A 1220 source : AC3 5) chain A residue 197 type sequence E description BINDING SITE FOR RESIDUE MES A 1220 source : AC3 6) chain A residue 7 type sequence Y description BINDING SITE FOR RESIDUE GSH A 1221 source : AC4 7) chain A residue 8 type sequence F description BINDING SITE FOR RESIDUE GSH A 1221 source : AC4 8) chain A residue 13 type sequence R description BINDING SITE FOR RESIDUE GSH A 1221 source : AC4 9) chain A residue 38 type sequence W description BINDING SITE FOR RESIDUE GSH A 1221 source : AC4 10) chain A residue 44 type sequence K description BINDING SITE FOR RESIDUE GSH A 1221 source : AC4 11) chain A residue 51 type sequence Q description BINDING SITE FOR RESIDUE GSH A 1221 source : AC4 12) chain A residue 52 type sequence L description BINDING SITE FOR RESIDUE GSH A 1221 source : AC4 13) chain A residue 64 type sequence Q description BINDING SITE FOR RESIDUE GSH A 1221 source : AC4 14) chain A residue 65 type sequence S description BINDING SITE FOR RESIDUE GSH A 1221 source : AC4 15) chain A residue 7 type sequence Y description BINDING SITE FOR RESIDUE NO A 1223 source : AC5 16) chain A residue 12 type sequence G description BINDING SITE FOR RESIDUE NO A 1223 source : AC5 17) chain A residue 13 type sequence R description BINDING SITE FOR RESIDUE NO A 1223 source : AC5 18) chain A residue 104 type sequence I description BINDING SITE FOR RESIDUE NO A 1223 source : AC5 19) chain A residue 7 type sequence Y description BINDING SITE FOR RESIDUE NO A 1224 source : AC6 20) chain A residue 8 type sequence F description BINDING SITE FOR RESIDUE NO A 1224 source : AC6 21) chain A residue 108 type sequence Y description BINDING SITE FOR RESIDUE NO A 1224 source : AC6 22) chain A residue 172 type sequence A description BINDING SITE FOR RESIDUE MES B 2220 source : AC7 23) chain A residue 98 type sequence D description BINDING SITE FOR RESIDUE GSH B 2221 source : AC8 24) chain A 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 25) chain A 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 26) chain A 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 27) chain A 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 28) chain A 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 29) chain A 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 30) chain A residue 4 type MOD_RES sequence T description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954 source Swiss-Prot : SWS_FT_FI2 31) chain A residue 199 type MOD_RES sequence V description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954 source Swiss-Prot : SWS_FT_FI2 32) chain A residue 128 type MOD_RES sequence P description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI5 33) chain A residue 62 type MOD_RES sequence L description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 34) chain A residue 103 type MOD_RES sequence Y description N6-succinyllysine => ECO:0000250|UniProtKB:P19157 source Swiss-Prot : SWS_FT_FI4 35) chain A residue 116 type MOD_RES sequence D description N6-succinyllysine => ECO:0000250|UniProtKB:P19157 source Swiss-Prot : SWS_FT_FI4

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