eF-site ID 1glp-A PDB Code 1glp Chain A 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 Mus musculus (Mouse) (GSTP1_MOUSE) Sequence A:  PPYTIVYFPVRGRCEAMRMLLADQGQSWKEEVVTIDTWMQ GLLKPTCLYGQLPKFEDGDLTLYQSNAILRHLGRSLGLYG KNQREAAQMDMVNDGVEDLRGKYVTLIYTNYENGKNDYVK ALPGHLKPFETLLSQNQGGKAFIVGDQISFADYNLLDLLL IHQVLAPGCLDNFPLLSAYVARLSARPKIKAFLSSPEHVN RPINGNGKQ Description Functional site 1) chain A residue 7 type sequence Y description source : GA 2) chain A residue 38 type sequence W description source : GA 3) chain A residue 44 type sequence K description source : GA 4) chain A residue 51 type sequence Q description source : GA 5) chain A residue 52 type sequence L description source : GA 6) chain A residue 64 type sequence Q description source : GA 7) chain A residue 65 type sequence S description source : GA 8) chain A residue 8 type sequence F description source : HA 9) chain A residue 10 type sequence V description source : HA 10) chain A residue 35 type sequence I description source : HA 11) chain A residue 108 type sequence Y description source : HA 12) chain A residue 205 type sequence G description source : HA 13) chain A residue 98 type sequence D description source : GB 14) chain A residue 7 type sequence Y description BINDING SITE FOR RESIDUE GTS A 210 source : AC1 15) chain A residue 8 type sequence F description BINDING SITE FOR RESIDUE GTS A 210 source : AC1 16) chain A residue 13 type sequence R description BINDING SITE FOR RESIDUE GTS A 210 source : AC1 17) chain A residue 38 type sequence W description BINDING SITE FOR RESIDUE GTS A 210 source : AC1 18) chain A residue 44 type sequence K description BINDING SITE FOR RESIDUE GTS A 210 source : AC1 19) chain A residue 51 type sequence Q description BINDING SITE FOR RESIDUE GTS A 210 source : AC1 20) chain A residue 52 type sequence L description BINDING SITE FOR RESIDUE GTS A 210 source : AC1 21) chain A residue 53 type sequence P description BINDING SITE FOR RESIDUE GTS A 210 source : AC1 22) chain A residue 64 type sequence Q description BINDING SITE FOR RESIDUE GTS A 210 source : AC1 23) chain A residue 65 type sequence S description BINDING SITE FOR RESIDUE GTS A 210 source : AC1 24) chain A residue 36 type sequence D description BINDING SITE FOR RESIDUE GTS B 210 source : AC2 25) chain A residue 39 type sequence M description BINDING SITE FOR RESIDUE GTS B 210 source : AC2 26) chain A residue 98 type sequence D description BINDING SITE FOR RESIDUE GTS B 210 source : AC2 27) chain A residue 8 type BINDING sequence F description BINDING => ECO:0000305|PubMed:8145243 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 14 type BINDING sequence C description BINDING => ECO:0000305|PubMed:8145243 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 39 type BINDING sequence M description BINDING => ECO:0000305|PubMed:8145243 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 45 type BINDING sequence P description BINDING => ECO:0000305|PubMed:8145243 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 52 type BINDING sequence L description BINDING => ECO:0000305|PubMed:8145243 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 65 type BINDING sequence S description BINDING => ECO:0000305|PubMed:8145243 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 4 type MOD_RES sequence T description Phosphotyrosine; by EGFR => ECO:0000250|UniProtKB:P09211 source Swiss-Prot : SWS_FT_FI2 34) chain A residue 62 type MOD_RES sequence L description Phosphothreonine => ECO:0000250|UniProtKB:P09211 source Swiss-Prot : SWS_FT_FI3 35) chain A residue 103 type MOD_RES sequence Y description N6-succinyllysine => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI4 36) chain A residue 116 type MOD_RES sequence N description N6-succinyllysine => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI4 37) chain A residue 128 type MOD_RES sequence P description N6-acetyllysine => ECO:0000250|UniProtKB:P09211 source Swiss-Prot : SWS_FT_FI5

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