eF-site ID 5ddl-AB PDB Code 5ddl Chain A, B click to enlarge Title Crystal Structure of WT Human Glutathione Transferase Pi soaked with a metalloid then back-soaked with glutathione Classification TRANSFERASE Compound Glutathione S-transferase P Source Homo sapiens (Human) (GSTP1_HUMAN) Sequence A:  MPPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQ EGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLY GKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYV KALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLL LIHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYV NLPINGNGKQ B:  PPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQE GSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYG KDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVK ALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLL IHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVN LPINGNGKQ Description Functional site 1) chain A residue 22 type sequence A description binding site for residue MES A 301 source : AC1 2) chain A residue 28 type sequence W description binding site for residue MES A 301 source : AC1 3) chain A residue 30 type sequence E description binding site for residue MES A 301 source : AC1 4) chain A residue 197 type sequence E description binding site for residue MES A 301 source : AC1 5) chain A residue 8 type sequence F description binding site for residue 5AU A 302 source : AC2 6) chain A residue 13 type sequence R description binding site for residue 5AU A 302 source : AC2 7) chain A residue 38 type sequence W description binding site for residue 5AU A 302 source : AC2 8) chain A residue 44 type sequence K description binding site for residue 5AU A 302 source : AC2 9) chain A residue 50 type sequence G description binding site for residue 5AU A 302 source : AC2 10) chain A residue 51 type sequence Q description binding site for residue 5AU A 302 source : AC2 11) chain A residue 52 type sequence L description binding site for residue 5AU A 302 source : AC2 12) chain A residue 53 type sequence P description binding site for residue 5AU A 302 source : AC2 13) chain A residue 64 type sequence Q description binding site for residue 5AU A 302 source : AC2 14) chain A residue 65 type sequence S description binding site for residue 5AU A 302 source : AC2 15) chain A residue 104 type sequence I description binding site for residue 5AU A 302 source : AC2 16) chain A residue 108 type sequence Y description binding site for residue 5AU A 302 source : AC2 17) chain B residue 98 type sequence D description binding site for residue 5AU A 302 source : AC2 18) chain B residue 102 type sequence K description binding site for residue 5AU A 302 source : AC2 19) chain A residue 7 type sequence Y description binding site for residue GSH A 303 source : AC3 20) chain A residue 8 type sequence F description binding site for residue GSH A 303 source : AC3 21) chain A residue 13 type sequence R description binding site for residue GSH A 303 source : AC3 22) chain A residue 38 type sequence W description binding site for residue GSH A 303 source : AC3 23) chain A residue 44 type sequence K description binding site for residue GSH A 303 source : AC3 24) chain A residue 50 type sequence G description binding site for residue GSH A 303 source : AC3 25) chain A residue 51 type sequence Q description binding site for residue GSH A 303 source : AC3 26) chain A residue 52 type sequence L description binding site for residue GSH A 303 source : AC3 27) chain A residue 53 type sequence P description binding site for residue GSH A 303 source : AC3 28) chain A residue 64 type sequence Q description binding site for residue GSH A 303 source : AC3 29) chain A residue 65 type sequence S description binding site for residue GSH A 303 source : AC3 30) chain B residue 98 type sequence D description binding site for residue GSH A 303 source : AC3 31) chain B residue 22 type sequence A description binding site for residue MES B 301 source : AC4 32) chain B residue 28 type sequence W description binding site for residue MES B 301 source : AC4 33) chain B residue 197 type sequence E description binding site for residue MES B 301 source : AC4 34) chain B residue 27 type sequence S description binding site for residue SO4 B 302 source : AC5 35) chain B residue 28 type sequence W description binding site for residue SO4 B 302 source : AC5 36) chain A residue 98 type sequence D description binding site for residue 5AU B 303 source : AC6 37) chain B residue 7 type sequence Y description binding site for residue 5AU B 303 source : AC6 38) chain B residue 8 type sequence F description binding site for residue 5AU B 303 source : AC6 39) chain B residue 10 type sequence V description binding site for residue 5AU B 303 source : AC6 40) chain B residue 13 type sequence R description binding site for residue 5AU B 303 source : AC6 41) chain B residue 38 type sequence W description binding site for residue 5AU B 303 source : AC6 42) chain B residue 44 type sequence K description binding site for residue 5AU B 303 source : AC6 43) chain B residue 50 type sequence G description binding site for residue 5AU B 303 source : AC6 44) chain B residue 51 type sequence Q description binding site for residue 5AU B 303 source : AC6 45) chain B residue 52 type sequence L description binding site for residue 5AU B 303 source : AC6 46) chain B residue 53 type sequence P description binding site for residue 5AU B 303 source : AC6 47) chain B residue 64 type sequence Q description binding site for residue 5AU B 303 source : AC6 48) chain B residue 65 type sequence S description binding site for residue 5AU B 303 source : AC6 49) chain B residue 104 type sequence I description binding site for residue 5AU B 303 source : AC6 50) chain B residue 108 type sequence Y description binding site for residue 5AU B 303 source : AC6 51) chain A residue 98 type sequence D description binding site for residue GSH B 304 source : AC7 52) chain B residue 7 type sequence Y description binding site for residue GSH B 304 source : AC7 53) chain B residue 8 type sequence F description binding site for residue GSH B 304 source : AC7 54) chain B residue 13 type sequence R description binding site for residue GSH B 304 source : AC7 55) chain B residue 38 type sequence W description binding site for residue GSH B 304 source : AC7 56) chain B residue 44 type sequence K description binding site for residue GSH B 304 source : AC7 57) chain B residue 50 type sequence G description binding site for residue GSH B 304 source : AC7 58) chain B residue 51 type sequence Q description binding site for residue GSH B 304 source : AC7 59) chain B residue 52 type sequence L description binding site for residue GSH B 304 source : AC7 60) chain B residue 53 type sequence P description binding site for residue GSH B 304 source : AC7 61) chain B residue 64 type sequence Q description binding site for residue GSH B 304 source : AC7 62) chain B residue 65 type sequence S description binding site for residue GSH B 304 source : AC7 63) chain B residue 77 type sequence G description binding site for residue CA B 305 source : AC8 64) chain B residue 147 type sequence Q description binding site for residue CA B 305 source : AC8 65) chain A residue 171 type sequence D description binding site for residue CA B 306 source : AC9 66) chain B residue 30 type sequence E description binding site for residue CA B 306 source : AC9 67) chain A residue 3 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954 source Swiss-Prot : SWS_FT_FI2 68) chain A residue 198 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954 source Swiss-Prot : SWS_FT_FI2 69) chain B residue 3 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954 source Swiss-Prot : SWS_FT_FI2 70) chain B residue 198 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954 source Swiss-Prot : SWS_FT_FI2 71) 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 72) 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 73) 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 74) 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 75) 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 76) 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 77) 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 78) 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 79) 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 80) 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 81) 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 82) 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 83) chain A residue 61 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 84) chain B residue 61 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 85) chain A residue 102 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P19157 source Swiss-Prot : SWS_FT_FI4 86) chain A residue 115 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P19157 source Swiss-Prot : SWS_FT_FI4 87) chain B residue 102 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P19157 source Swiss-Prot : SWS_FT_FI4 88) chain B residue 115 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P19157 source Swiss-Prot : SWS_FT_FI4 89) chain A residue 127 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI5 90) 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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