eF-site ID 5ddl-B PDB Code 5ddl Chain 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 B:  PPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQE GSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYG KDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVK ALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLL IHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVN LPINGNGKQ Description Functional site 1) chain B residue 98 type sequence D description binding site for residue 5AU A 302 source : AC2 2) chain B residue 102 type sequence K description binding site for residue 5AU A 302 source : AC2 3) chain B residue 98 type sequence D description binding site for residue GSH A 303 source : AC3 4) chain B residue 22 type sequence A description binding site for residue MES B 301 source : AC4 5) chain B residue 28 type sequence W description binding site for residue MES B 301 source : AC4 6) chain B residue 197 type sequence E description binding site for residue MES B 301 source : AC4 7) chain B residue 27 type sequence S description binding site for residue SO4 B 302 source : AC5 8) chain B residue 28 type sequence W description binding site for residue SO4 B 302 source : AC5 9) chain B residue 7 type sequence Y description binding site for residue 5AU B 303 source : AC6 10) chain B residue 8 type sequence F description binding site for residue 5AU B 303 source : AC6 11) chain B residue 10 type sequence V description binding site for residue 5AU B 303 source : AC6 12) chain B residue 13 type sequence R description binding site for residue 5AU B 303 source : AC6 13) chain B residue 38 type sequence W description binding site for residue 5AU B 303 source : AC6 14) chain B residue 44 type sequence K description binding site for residue 5AU B 303 source : AC6 15) chain B residue 50 type sequence G description binding site for residue 5AU B 303 source : AC6 16) chain B residue 51 type sequence Q description binding site for residue 5AU B 303 source : AC6 17) chain B residue 52 type sequence L description binding site for residue 5AU B 303 source : AC6 18) chain B residue 53 type sequence P description binding site for residue 5AU B 303 source : AC6 19) chain B residue 64 type sequence Q description binding site for residue 5AU B 303 source : AC6 20) chain B residue 65 type sequence S description binding site for residue 5AU B 303 source : AC6 21) chain B residue 104 type sequence I description binding site for residue 5AU B 303 source : AC6 22) chain B residue 108 type sequence Y description binding site for residue 5AU B 303 source : AC6 23) chain B residue 7 type sequence Y description binding site for residue GSH B 304 source : AC7 24) chain B residue 8 type sequence F description binding site for residue GSH B 304 source : AC7 25) chain B residue 13 type sequence R description binding site for residue GSH B 304 source : AC7 26) chain B residue 38 type sequence W description binding site for residue GSH B 304 source : AC7 27) chain B residue 44 type sequence K description binding site for residue GSH B 304 source : AC7 28) chain B residue 50 type sequence G description binding site for residue GSH B 304 source : AC7 29) chain B residue 51 type sequence Q description binding site for residue GSH B 304 source : AC7 30) chain B residue 52 type sequence L description binding site for residue GSH B 304 source : AC7 31) chain B residue 53 type sequence P description binding site for residue GSH B 304 source : AC7 32) chain B residue 64 type sequence Q description binding site for residue GSH B 304 source : AC7 33) chain B residue 65 type sequence S description binding site for residue GSH B 304 source : AC7 34) chain B residue 77 type sequence G description binding site for residue CA B 305 source : AC8 35) chain B residue 147 type sequence Q description binding site for residue CA B 305 source : AC8 36) chain B residue 30 type sequence E description binding site for residue CA B 306 source : AC9 37) chain B residue 3 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954 source Swiss-Prot : SWS_FT_FI2 38) chain B residue 198 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954 source Swiss-Prot : SWS_FT_FI2 39) 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 40) 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 41) 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 42) 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 43) 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 44) 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 45) chain B residue 61 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 46) chain B residue 102 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P19157 source Swiss-Prot : SWS_FT_FI4 47) chain B residue 115 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P19157 source Swiss-Prot : SWS_FT_FI4 48) 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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