eF-site ID 2hwg-A PDB Code 2hwg Chain A click to enlarge Title Structure of phosphorylated Enzyme I of the phosphoenolpyruvate:sugar phosphotransferase system Classification TRANSFERASE Compound Phosphoenolpyruvate-protein phosphotransferase Source (PT1_ECOLI) Sequence A:  ISGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEVE RFLSGRAKASAQLETIKTKAGETFGEEKEAIFEGHIXLLE DEELEQEIIALIKDKHXTADAAAHEVIEGQASALEELDDE YLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVAA DLTPSETAQLNLKKVLGFITDAGGRTSXTSIXARSLELPA IVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKXRA VQEQVASEKAELAKLKDLPAITLDGHQVEVCANIGTVRDV EGAERNGAEGVGLYRTEFLFXDRDALPTEEEQFAAYKAVA EACGSQAVIVRTXDIGGDKELPYXNFPKEENPFLGWRAIR IAXDRREILRDQLRAILRASAFGKLRIXFPXIISVEEVRA LRKEIEIYKQELRDEGKAFDESIEIGVXVETPAAATIARH LAKEVDFFSIGTNDLTQYTLAVDRGNDXISHLYQPXSPSV LNLIKQVIDASHAEGKWTGXCGELAGDERATLLLLGXGLD EFSXSAISIPRIKKIIRNTNFEDAKVLAEQALAQPTTDEL XTLVNKFIEEKT Description Functional site 1) chain A residue 189 type sequence X description BINDING SITE FOR RESIDUE MG A 901 source : AC1 2) chain A residue 358 type sequence R description BINDING SITE FOR RESIDUE MG A 901 source : AC1 3) chain A residue 431 type sequence E description BINDING SITE FOR RESIDUE MG A 901 source : AC1 4) chain A residue 455 type sequence D description BINDING SITE FOR RESIDUE MG A 901 source : AC1 5) chain A residue 189 type sequence X description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 6) chain A residue 296 type sequence R description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 7) chain A residue 332 type sequence R description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 8) chain A residue 429 type sequence X description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 9) chain A residue 431 type sequence E description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 10) chain A residue 452 type sequence G description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 11) chain A residue 453 type sequence T description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 12) chain A residue 454 type sequence N description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 13) chain A residue 455 type sequence D description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 14) chain A residue 465 type sequence R description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 15) chain A residue 502 type sequence C description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 16) chain A residue 503 type sequence G description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 17) chain A residue 189 type catalytic sequence X description 920 source MCSA : MCSA1 18) chain A residue 431 type catalytic sequence E description 920 source MCSA : MCSA1 19) chain A residue 455 type catalytic sequence D description 920 source MCSA : MCSA1 20) chain A residue 502 type catalytic sequence C description 920 source MCSA : MCSA1 21) chain A residue 502 type ACT_SITE sequence C description Proton donor => ECO:0000269|PubMed:12705838, ECO:0000305|PubMed:17053069 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 296 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P23533 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 465 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P23533 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 332 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 431 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 26) chain A residue 454 type BINDING sequence N description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 27) chain A residue 455 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 28) chain A residue 184-195 type prosite sequence GGRTSXTSIXAR description PEP_ENZYMES_PHOS_SITE PEP-utilizing enzymes phosphorylation site signature. GGrTsHTSIMAR source prosite : PS00370 29) chain A residue 447-465 type prosite sequence DFFSIGTNDLTQYTLAVDR description PEP_ENZYMES_2 PEP-utilizing enzymes signature 2. DfFSIGTNDLtQYTLAvdR source prosite : PS00742 30) chain A residue 189 type ACT_SITE sequence X description Tele-phosphohistidine intermediate => ECO:0000269|PubMed:12705838, ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI1

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