eF-site ID 3d54-A PDB Code 3d54 Chain A click to enlarge Title Structure of PurLQS from Thermotoga maritima Classification LIGASE Compound Phosphoribosylformylglycinamidine synthase II Source Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) (PURQ_THEMA) Sequence A:  KLRYLNILKEKLGREPTFVELQAFSVMWSEHCGYSHTKKY IRRLPKTGNAGVVNLDDYYSVAFKIESHNHPSAIEPYNGA ATGVGGIIRDVLAMGARPTAIFDSLHMSRIIDGIIEGIAD YGNSIGVPTVGGELRISSLYAHNPLVNVLAAGVVRNDMLV DSKASRPGQVIVIFGGATGRDGTKLSIQVGDPFAEKMLIE AFLEMVEEGLVEGAQDLGAGGVLSATSELVAKGNLGAIVH LDRVPLREPDMEPWEILISESQERMAVVTSPQKASRILEI ARKHLLFGDVVAEVIEEPVYRVMYRNDLVMEVPVQLLANA PEEDIVEYTPGKIPEFKRVEFEEVNAREVFEQYDHMVGTD TVVPPGFGAAVMRIKRDGGYSLVTHSRADLALQDTYWGTL IAVLESVRKTLSVGAEPLAITNCVNYGDPDVDPVGLSAMM TALKNACEFSGVPVASGNASLYNTYQGKPIPPTLVVGMLG KVNPQKVAKPKPSKVFAVGWNDFELEREKELWRAIRKLSE EGAFILSSSQLLTRTHVETFREYGLKIEVKLPEVRPAHQM VLVFSERTPVVDVPVKEIGTLSR Description (1)  Phosphoribosylformylglycinamidine synthase II (E.C.6.3.5.3), Formylglycinamide ribonucleotide amidotransferase, PurS, Phosphoribosylformylglycinamidine synthase 1 (E.C.6.3.5.3) Functional site 1) chain A residue 94 type sequence D description BINDING SITE FOR RESIDUE NA A 3003 source : AC1 2) chain A residue 236 type sequence D description BINDING SITE FOR RESIDUE NA A 3003 source : AC1 3) chain A residue 107 type sequence D description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 4) chain A residue 135 type sequence G description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 5) chain A residue 136 type sequence G description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 6) chain A residue 137 type sequence E description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 7) chain A residue 138 type sequence L description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 8) chain A residue 139 type sequence R description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 9) chain A residue 366 type sequence A description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 10) chain A residue 370 type sequence F description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 11) chain A residue 373 type sequence Y description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 12) chain A residue 385 type sequence P description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 13) chain A residue 386 type sequence G description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 14) chain A residue 388 type sequence G description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 15) chain A residue 429 type sequence K description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 16) chain A residue 548 type sequence S description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 17) chain A residue 553 type sequence T description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 18) chain A residue 555 type sequence T description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 19) chain A residue 556 type sequence H description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 20) chain A residue 35 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 68 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 442 type BINDING sequence N description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 source Swiss-Prot : SWS_FT_FI3 23) 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 24) 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 25) 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 26) 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 27) chain A residue 71 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI5 28) chain A residue 93 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI5 29) chain A residue 136 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI5 30) chain A residue 208 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI5 31) chain A residue 280 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI5 32) chain A residue 480 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI5 33) chain A residue 107 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 34) chain A residue 388 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 35) chain A residue 429 type BINDING sequence K description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 36) chain A residue 549 type BINDING sequence S description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 37) chain A residue 556 type BINDING sequence H description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 38) chain A residue 246-258 type prosite sequence TSELVAKGNLGAI description PTR2_2 PTR2 family proton/oligopeptide symporters signature 2. TseLVAkGNLGAI source prosite : PS01023 39) 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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