eF-site ID 2hwg-AB PDB Code 2hwg Chain A, B 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 B:  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 B residue 189 type sequence X description BINDING SITE FOR RESIDUE MG B 902 source : AC2 6) chain B residue 358 type sequence R description BINDING SITE FOR RESIDUE MG B 902 source : AC2 7) chain B residue 431 type sequence E description BINDING SITE FOR RESIDUE MG B 902 source : AC2 8) chain B residue 455 type sequence D description BINDING SITE FOR RESIDUE MG B 902 source : AC2 9) chain B residue 465 type sequence R description BINDING SITE FOR RESIDUE MG B 902 source : AC2 10) chain A residue 189 type sequence X description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 11) chain A residue 296 type sequence R description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 12) chain A residue 332 type sequence R description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 13) chain A residue 429 type sequence X description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 14) chain A residue 431 type sequence E description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 15) chain A residue 452 type sequence G description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 16) chain A residue 453 type sequence T description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 17) chain A residue 454 type sequence N description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 18) chain A residue 455 type sequence D description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 19) chain A residue 465 type sequence R description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 20) chain A residue 502 type sequence C description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 21) chain A residue 503 type sequence G description BINDING SITE FOR RESIDUE OXL A 903 source : AC3 22) chain B residue 189 type sequence X description BINDING SITE FOR RESIDUE OXL B 904 source : AC4 23) chain B residue 296 type sequence R description BINDING SITE FOR RESIDUE OXL B 904 source : AC4 24) chain B residue 332 type sequence R description BINDING SITE FOR RESIDUE OXL B 904 source : AC4 25) chain B residue 429 type sequence X description BINDING SITE FOR RESIDUE OXL B 904 source : AC4 26) chain B residue 431 type sequence E description BINDING SITE FOR RESIDUE OXL B 904 source : AC4 27) chain B residue 452 type sequence G description BINDING SITE FOR RESIDUE OXL B 904 source : AC4 28) chain B residue 453 type sequence T description BINDING SITE FOR RESIDUE OXL B 904 source : AC4 29) chain B residue 454 type sequence N description BINDING SITE FOR RESIDUE OXL B 904 source : AC4 30) chain B residue 455 type sequence D description BINDING SITE FOR RESIDUE OXL B 904 source : AC4 31) chain B residue 465 type sequence R description BINDING SITE FOR RESIDUE OXL B 904 source : AC4 32) chain B residue 503 type sequence G description BINDING SITE FOR RESIDUE OXL B 904 source : AC4 33) chain A residue 189 type catalytic sequence X description 920 source MCSA : MCSA1 34) chain A residue 431 type catalytic sequence E description 920 source MCSA : MCSA1 35) chain A residue 455 type catalytic sequence D description 920 source MCSA : MCSA1 36) chain A residue 502 type catalytic sequence C description 920 source MCSA : MCSA1 37) chain B residue 189 type catalytic sequence X description 920 source MCSA : MCSA2 38) chain B residue 431 type catalytic sequence E description 920 source MCSA : MCSA2 39) chain B residue 455 type catalytic sequence D description 920 source MCSA : MCSA2 40) chain B residue 502 type catalytic sequence C description 920 source MCSA : MCSA2 41) chain A residue 184-195 type prosite sequence GGRTSXTSIXAR description PEP_ENZYMES_PHOS_SITE PEP-utilizing enzymes phosphorylation site signature. GGrTsHTSIMAR source prosite : PS00370 42) chain A residue 447-465 type prosite sequence DFFSIGTNDLTQYTLAVDR description PEP_ENZYMES_2 PEP-utilizing enzymes signature 2. DfFSIGTNDLtQYTLAvdR source prosite : PS00742 43) 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 44) chain B 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 45) 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 46) chain B residue 502 type ACT_SITE sequence C description Proton donor => ECO:0000269|PubMed:12705838, ECO:0000305|PubMed:17053069 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 296 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P23533 source Swiss-Prot : SWS_FT_FI3 48) chain A residue 465 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P23533 source Swiss-Prot : SWS_FT_FI3 49) chain B residue 296 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P23533 source Swiss-Prot : SWS_FT_FI3 50) chain B residue 465 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P23533 source Swiss-Prot : SWS_FT_FI3 51) chain A residue 332 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 52) chain A residue 431 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 53) chain A residue 454 type BINDING sequence N description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 54) chain A residue 455 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 55) chain B residue 332 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 56) chain B residue 431 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 57) chain B residue 454 type BINDING sequence N description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 58) chain B residue 455 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4

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