eF-site ID 2hs3-A PDB Code 2hs3 Chain A click to enlarge Title T. maritima PurL complexed with FGAR Classification LIGASE Compound Phosphoribosylformylglycinamidine synthase II Source Thermotoga maritima (PURL_THEMA) Sequence A:  KLRYLNILKEKLGREPTFVELQAFSVMWSEHCGYSHTKKY IRRLPKTGFEGNAGVVNLDDYYSVAFKIESHNHPSAIEPY NGAATGVGGIIRDVLAMGARPTAIFDSLHMSRIIDGIIEG IADYGNSIGVPTVGGELRISSLYAHNPLVNVLAAGVVRND MLVDSKASRPGQVIVIFGGATGRDGIHGASFASEDLTGDK ATKLSIQVGDPFAEKMLIEAFLEMVEEGLVEGAQDLGAGG VLSATSELVAKGNLGAIVHLDRVPLREPDMEPWEILISES QERMAVVTSPQKASRILEIARKHLLFGDVVAEVIEEPVYR VMYRNDLVMEVPVQLLANAPEEDIVEYTPGKIPEFKRVEF EEVNAREVFEQYDHMVGTDTVVPPGFGAAVMRIKRDGGYS LVTHSRADLALQDTYWGTLIAVLESVRKTLSVGAEPLAIT NCVNYGDPDVDPVGLSAMMTALKNACEFSGVPVASGNASL YNTYQGKPIPPTLVVGMLGKVNPQKVAKPKPSKVFAVGWN DFELEREKELWRAIRKLSEEGAFILSSSQLLTRTHVETFR EYGLKIEVKLPEVRPAHQMVLVFSERTPVVDVPVKEIGTL SR Description Functional site 1) chain A residue 139 type sequence R description BINDING SITE FOR RESIDUE PO4 A 905 source : AC1 2) chain A residue 363 type sequence E description BINDING SITE FOR RESIDUE PO4 A 905 source : AC1 3) chain A residue 405 type sequence H description BINDING SITE FOR RESIDUE PO4 A 905 source : AC1 4) chain A residue 429 type sequence K description BINDING SITE FOR RESIDUE PO4 A 905 source : AC1 5) chain A residue 548 type sequence S description BINDING SITE FOR RESIDUE PO4 A 905 source : AC1 6) chain A residue 549 type sequence S description BINDING SITE FOR RESIDUE PO4 A 905 source : AC1 7) chain A residue 32 type sequence H description BINDING SITE FOR RESIDUE FGR A 2166 source : AC2 8) chain A residue 71 type sequence S description BINDING SITE FOR RESIDUE FGR A 2166 source : AC2 9) chain A residue 72 type sequence H description BINDING SITE FOR RESIDUE FGR A 2166 source : AC2 10) chain A residue 73 type sequence N description BINDING SITE FOR RESIDUE FGR A 2166 source : AC2 11) chain A residue 74 type sequence H description BINDING SITE FOR RESIDUE FGR A 2166 source : AC2 12) chain A residue 75 type sequence P description BINDING SITE FOR RESIDUE FGR A 2166 source : AC2 13) chain A residue 86 type sequence T description BINDING SITE FOR RESIDUE FGR A 2166 source : AC2 14) chain A residue 90 type sequence G description BINDING SITE FOR RESIDUE FGR A 2166 source : AC2 15) chain A residue 93 type sequence R description BINDING SITE FOR RESIDUE FGR A 2166 source : AC2 16) chain A residue 189 type sequence G description BINDING SITE FOR RESIDUE FGR A 2166 source : AC2 17) chain A residue 190 type sequence A description BINDING SITE FOR RESIDUE FGR A 2166 source : AC2 18) chain A residue 193 type sequence A description BINDING SITE FOR RESIDUE FGR A 2166 source : AC2 19) chain A residue 208 type sequence Q description BINDING SITE FOR RESIDUE FGR A 2166 source : AC2 20) chain A residue 239 type sequence A description BINDING SITE FOR RESIDUE FGR A 2166 source : AC2 21) chain A residue 280 type sequence E description BINDING SITE FOR RESIDUE FGR A 2166 source : AC2 22) chain A residue 282 type sequence Q description BINDING SITE FOR RESIDUE FGR A 2166 source : AC2 23) chain A residue 480 type sequence S description BINDING SITE FOR RESIDUE FGR A 2166 source : AC2 24) chain A residue 246-258 type prosite sequence TSELVAKGNLGAI description PTR2_2 PTR2 family proton/oligopeptide symporters signature 2. TseLVAkGNLGAI source prosite : PS01023 25) chain A residue 32 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 72 type ACT_SITE sequence H description Proton acceptor => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 35 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 source Swiss-Prot : SWS_FT_FI3 28) chain A residue 68 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 source Swiss-Prot : SWS_FT_FI3 29) chain A residue 442 type BINDING sequence N description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 70 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526 source Swiss-Prot : SWS_FT_FI4 31) chain A residue 94 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526 source Swiss-Prot : SWS_FT_FI4 32) chain A residue 236 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526 source Swiss-Prot : SWS_FT_FI4 33) chain A residue 478 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526 source Swiss-Prot : SWS_FT_FI4 34) chain A residue 71 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI5 35) chain A residue 93 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI5 36) chain A residue 136 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI5 37) chain A residue 189 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI5 38) chain A residue 208 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI5 39) chain A residue 280 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI5 40) chain A residue 480 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI5 41) chain A residue 107 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 42) chain A residue 388 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 43) chain A residue 429 type BINDING sequence K description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 44) chain A residue 549 type BINDING sequence S description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 45) chain A residue 556 type BINDING sequence H description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 46) chain A residue 477 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 source Swiss-Prot : SWS_FT_FI7

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