eF-site ID 3d54-I PDB Code 3d54 Chain I 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 I:  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 I residue 94 type sequence D description BINDING SITE FOR RESIDUE NA I 3001 source : AC2 2) chain I residue 236 type sequence D description BINDING SITE FOR RESIDUE NA I 3001 source : AC2 3) chain I residue 107 type sequence D description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 4) chain I residue 135 type sequence G description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 5) chain I residue 136 type sequence G description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 6) chain I residue 137 type sequence E description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 7) chain I residue 138 type sequence L description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 8) chain I residue 139 type sequence R description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 9) chain I residue 366 type sequence A description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 10) chain I residue 370 type sequence F description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 11) chain I residue 373 type sequence Y description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 12) chain I residue 385 type sequence P description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 13) chain I residue 386 type sequence G description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 14) chain I residue 388 type sequence G description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 15) chain I residue 429 type sequence K description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 16) chain I residue 548 type sequence S description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 17) chain I residue 553 type sequence T description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 18) chain I residue 555 type sequence T description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 19) chain I residue 556 type sequence H description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 20) chain I residue 35 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 source Swiss-Prot : SWS_FT_FI3 21) chain I residue 68 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 source Swiss-Prot : SWS_FT_FI3 22) chain I residue 442 type BINDING sequence N description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 source Swiss-Prot : SWS_FT_FI3 23) chain I residue 94 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526 source Swiss-Prot : SWS_FT_FI4 24) chain I residue 236 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526 source Swiss-Prot : SWS_FT_FI4 25) chain I residue 478 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526 source Swiss-Prot : SWS_FT_FI4 26) chain I residue 70 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526 source Swiss-Prot : SWS_FT_FI4 27) chain I residue 71 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI5 28) chain I residue 93 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI5 29) chain I residue 136 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI5 30) chain I residue 208 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI5 31) chain I residue 280 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI5 32) chain I residue 480 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI5 33) chain I residue 107 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 34) chain I residue 388 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 35) chain I residue 429 type BINDING sequence K description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 36) chain I residue 549 type BINDING sequence S description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 37) chain I residue 556 type BINDING sequence H description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 38) chain I 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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