eF-site ID 2l5h_1-A PDB Code 2l5h Model 1 Chain A 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 null (PT1_ECOLI) Sequence A:  MISGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEV ERFLSGRAKASAQLETIKTKAGETFGEEKEAIFEGHIMLL EDEELEQEIIALIKDKHMTADAAAHEVIEGQASALEELDD EYLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVA ADLTPSETAQLNLKKVLGFITDAGGRTSQTSIMARSLELP AIVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKMR AVQEQVASEKAELAKLKDLPAITLDGHQVEVCANIGTVRD VEGAERNGAEGVGLYRTEFLFMDRDALPTEEEQFAAYKAV AEACGSQAVIVRTMDIGGDKELPYMNFPKEENPFLGWRAI RIAMDRREILRDQLRAILRASAFGKLRIMFPMIISVEEVR ALRKEIEIYKQELRDEGKAFDESIEIGVMVETPAAATIAR HLAKEVDFFSIGTNDLTQYTLAVDRGNDMISHLYQPMSPS VLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGL DEFSMSAISIPRIKKIIRNTNFEDAKVLAEQALAQPTTDE LMTLVNKFIEEKT Description (1)  Phosphoenolpyruvate-protein phosphotransferase (E.C.2.7.3.9) Functional site 1) 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 2) 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 3) chain A residue 296 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P23533 source Swiss-Prot : SWS_FT_FI3 4) chain A residue 465 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P23533 source Swiss-Prot : SWS_FT_FI3 5) chain A residue 431 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 6) chain A residue 454 type BINDING sequence N description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 7) chain A residue 455 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 8) chain A residue 332 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 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 catalytic sequence Q description 920 source MCSA : MCSA1 11) chain A residue 431 type catalytic sequence E description 920 source MCSA : MCSA1 12) chain A residue 455 type catalytic sequence D description 920 source MCSA : MCSA1 13) chain A residue 502 type catalytic sequence C description 920 source MCSA : MCSA1

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