eF-site ID 1glp-B PDB Code 1glp Chain B click to enlarge Title 1.8 ANGSTROMS MOLECULAR STRUCTURE OF MOUSE LIVER CLASS PI GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S-(P-NITROBENZYL)GLUTATHIONE AND OTHER INHIBITORS Classification TRANSFERASE(GLUTATHIONE) Compound GLUTATHIONE S-TRANSFERASE YFYF Source null (GSTP1_MOUSE) Sequence B:  PPYTIVYFPVRGRCEAMRMLLADQGQSWKEEVVTIDTWMQ GLLKPTCLYGQLPKFEDGDLTLYQSNAILRHLGRSLGLYG KNQREAAQMDMVNDGVEDLRGKYVTLIYTNYENGKNDYVK ALPGHLKPFETLLSQNQGGKAFIVGDQISFADYNLLDLLL IHQVLAPGCLDNFPLLSAYVARLSARPKIKAFLSSPEHVN RPINGNGKQ Description Functional site 1) chain B residue 98 type sequence D description source : GA 2) chain B residue 7 type sequence Y description source : GB 3) chain B residue 38 type sequence W description source : GB 4) chain B residue 44 type sequence K description source : GB 5) chain B residue 51 type sequence Q description source : GB 6) chain B residue 52 type sequence L description source : GB 7) chain B residue 64 type sequence Q description source : GB 8) chain B residue 65 type sequence S description source : GB 9) chain B residue 8 type sequence F description source : HB 10) chain B residue 10 type sequence V description source : HB 11) chain B residue 35 type sequence I description source : HB 12) chain B residue 108 type sequence Y description source : HB 13) chain B residue 205 type sequence G description source : HB 14) chain B residue 39 type sequence M description BINDING SITE FOR RESIDUE GTS A 210 source : AC1 15) chain B residue 98 type sequence D description BINDING SITE FOR RESIDUE GTS A 210 source : AC1 16) chain B residue 7 type sequence Y description BINDING SITE FOR RESIDUE GTS B 210 source : AC2 17) chain B residue 8 type sequence F description BINDING SITE FOR RESIDUE GTS B 210 source : AC2 18) chain B residue 13 type sequence R description BINDING SITE FOR RESIDUE GTS B 210 source : AC2 19) chain B residue 38 type sequence W description BINDING SITE FOR RESIDUE GTS B 210 source : AC2 20) chain B residue 44 type sequence K description BINDING SITE FOR RESIDUE GTS B 210 source : AC2 21) chain B residue 51 type sequence Q description BINDING SITE FOR RESIDUE GTS B 210 source : AC2 22) chain B residue 52 type sequence L description BINDING SITE FOR RESIDUE GTS B 210 source : AC2 23) chain B residue 64 type sequence Q description BINDING SITE FOR RESIDUE GTS B 210 source : AC2 24) chain B residue 65 type sequence S description BINDING SITE FOR RESIDUE GTS B 210 source : AC2 25) chain B residue 8 type BINDING sequence F description BINDING => ECO:0000305|PubMed:8145243 source Swiss-Prot : SWS_FT_FI1 26) chain B residue 14 type BINDING sequence C description BINDING => ECO:0000305|PubMed:8145243 source Swiss-Prot : SWS_FT_FI1 27) chain B residue 45 type BINDING sequence P description BINDING => ECO:0000305|PubMed:8145243 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 52 type BINDING sequence L description BINDING => ECO:0000305|PubMed:8145243 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 65 type BINDING sequence S description BINDING => ECO:0000305|PubMed:8145243 source Swiss-Prot : SWS_FT_FI1 30) chain B residue 39 type BINDING sequence M description BINDING => ECO:0000305|PubMed:8145243 source Swiss-Prot : SWS_FT_FI1 31) chain B residue 4 type MOD_RES sequence T description Phosphotyrosine; by EGFR => ECO:0000250|UniProtKB:P09211 source Swiss-Prot : SWS_FT_FI2 32) chain B residue 62 type MOD_RES sequence L description Phosphothreonine => ECO:0000250|UniProtKB:P09211 source Swiss-Prot : SWS_FT_FI3 33) chain B residue 103 type MOD_RES sequence Y description N6-succinyllysine => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI4 34) chain B residue 116 type MOD_RES sequence N description N6-succinyllysine => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI4 35) chain B residue 128 type MOD_RES sequence P description N6-acetyllysine => ECO:0000250|UniProtKB:P09211 source Swiss-Prot : SWS_FT_FI5

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