eF-site ID 2l5h_2-AB PDB Code 2l5h Model 2 Chain A, B click to enlarge Title Solution Structure of the H189Q mutant of the Enzyme I dimer Using Residual Dipolar Couplings and Small Angle X-Ray Scattering Classification TRANSFERASE Compound Phosphoenolpyruvate-protein phosphotransferase Source Escherichia coli (strain K12) (PT1_ECOLI) Sequence A:  MISGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEV ERFLSGRAKASAQLETIKTKAGETFGEEKEAIFEGHIMLL EDEELEQEIIALIKDKHMTADAAAHEVIEGQASALEELDD EYLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVA ADLTPSETAQLNLKKVLGFITDAGGRTSQTSIMARSLELP AIVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKMR AVQEQVASEKAELAKLKDLPAITLDGHQVEVCANIGTVRD VEGAERNGAEGVGLYRTEFLFMDRDALPTEEEQFAAYKAV AEACGSQAVIVRTMDIGGDKELPYMNFPKEENPFLGWRAI RIAMDRREILRDQLRAILRASAFGKLRIMFPMIISVEEVR ALRKEIEIYKQELRDEGKAFDESIEIGVMVETPAAATIAR HLAKEVDFFSIGTNDLTQYTLAVDRGNDMISHLYQPMSPS VLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGL DEFSMSAISIPRIKKIIRNTNFEDAKVLAEQALAQPTTDE LMTLVNKFIEEKT B:  MISGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEV ERFLSGRAKASAQLETIKTKAGETFGEEKEAIFEGHIMLL EDEELEQEIIALIKDKHMTADAAAHEVIEGQASALEELDD EYLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVA ADLTPSETAQLNLKKVLGFITDAGGRTSQTSIMARSLELP AIVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKMR AVQEQVASEKAELAKLKDLPAITLDGHQVEVCANIGTVRD VEGAERNGAEGVGLYRTEFLFMDRDALPTEEEQFAAYKAV AEACGSQAVIVRTMDIGGDKELPYMNFPKEENPFLGWRAI RIAMDRREILRDQLRAILRASAFGKLRIMFPMIISVEEVR ALRKEIEIYKQELRDEGKAFDESIEIGVMVETPAAATIAR HLAKEVDFFSIGTNDLTQYTLAVDRGNDMISHLYQPMSPS VLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGL DEFSMSAISIPRIKKIIRNTNFEDAKVLAEQALAQPTTDE LMTLVNKFIEEKT Description Functional site 1) chain A residue 189 type catalytic sequence Q description 920 source MCSA : MCSA1 2) chain A residue 431 type catalytic sequence E description 920 source MCSA : MCSA1 3) chain A residue 455 type catalytic sequence D description 920 source MCSA : MCSA1 4) chain A residue 502 type catalytic sequence C description 920 source MCSA : MCSA1 5) chain B residue 189 type catalytic sequence Q description 920 source MCSA : MCSA2 6) chain B residue 431 type catalytic sequence E description 920 source MCSA : MCSA2 7) chain B residue 455 type catalytic sequence D description 920 source MCSA : MCSA2 8) chain B residue 502 type catalytic sequence C description 920 source MCSA : MCSA2 9) chain A residue 447-465 type prosite sequence DFFSIGTNDLTQYTLAVDR description PEP_ENZYMES_2 PEP-utilizing enzymes signature 2. DfFSIGTNDLtQYTLAvdR source prosite : PS00742 10) chain A residue 189 type ACT_SITE sequence Q description Tele-phosphohistidine intermediate => ECO:0000269|PubMed:12705838, ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI1 11) chain B residue 189 type ACT_SITE sequence Q description Tele-phosphohistidine intermediate => ECO:0000269|PubMed:12705838, ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI1 12) 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 13) 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 14) chain A residue 296 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P23533 source Swiss-Prot : SWS_FT_FI3 15) chain A residue 465 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P23533 source Swiss-Prot : SWS_FT_FI3 16) chain B residue 296 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P23533 source Swiss-Prot : SWS_FT_FI3 17) chain B residue 465 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P23533 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 332 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 19) chain A residue 431 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 20) chain A residue 454 type BINDING sequence N description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 21) chain A residue 455 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 22) chain B residue 332 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 23) chain B residue 431 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 24) chain B residue 454 type BINDING sequence N description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 25) chain B residue 455 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4

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