eF-site ID 2l5h_2-B PDB Code 2l5h Model 2 Chain 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 B:  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 B residue 189 type catalytic sequence Q description 920 source MCSA : MCSA2 2) chain B residue 431 type catalytic sequence E description 920 source MCSA : MCSA2 3) chain B residue 455 type catalytic sequence D description 920 source MCSA : MCSA2 4) chain B residue 502 type catalytic sequence C description 920 source MCSA : MCSA2 5) 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 6) 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 7) chain B residue 296 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P23533 source Swiss-Prot : SWS_FT_FI3 8) chain B residue 465 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P23533 source Swiss-Prot : SWS_FT_FI3 9) chain B residue 332 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 10) chain B residue 431 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 11) chain B residue 454 type BINDING sequence N description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4 12) chain B residue 455 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17053069 source Swiss-Prot : SWS_FT_FI4

Display surface Download Links