eF-site ID 3d54-ABCDEFGHIJKL PDB Code 3d54 Chain A, B, C, D, E, F, G, H, I, J, K, L 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 B:  MPLFKFAIDVQYRSNVRDPRGETIERVLREEKGLPVKKLR LGKSIHLEVEAENKEKAYEIVKKACEELLVNPVVEEYEVR EL C:  MPLFKFAIDVQYRSNVRDPRGETIERVLREEKGLPVKKLR LGKSIHLEVEAENKEKAYEIVKKACEELLVNPVVEEYEVR EL D:  MKPRACVVVYPGSNCDRDAYHALEINGFEPSYVGLDDKLD DYELIILPGGFSYGDYLRPGAVAAREKIAFEIAKAAERGK LIMGIXNGFQILIEMGLLKGALLQNSSGKFICKWVDLIVE NNDTPFTNAFEKGEKIRIPIAHGFGRYVKIDDVNVVLRYV KDVNGSDERIAGVLNESGNVFGLMPHPERAVEELIGGEDG KKVFQSILNYLK E:  KLRYLNILKEKLGREPTFVELQAFSVMWSEHCGYSHTKKY IRRLPKTGNAGVVNLDDYYSVAFKIESHNHPSAIEPYNGA ATGVGGIIRDVLAMGARPTAIFDSLHMSRIIDGIIEGIAD YGNSIGVPTVGGELRISSLYAHNPLVNVLAAGVVRNDMLV DSKASRPGQVIVIFGGATGRDGTKLSIQVGDPFAEKMLIE AFLEMVEEGLVEGAQDLGAGGVLSATSELVAKGNLGAIVH LDRVPLREPDMEPWEILISESQERMAVVTSPQKASRILEI ARKHLLFGDVVAEVIEEPVYRVMYRNDLVMEVPVQLLANA PEEDIVEYTPGKIPEFKRVEFEEVNAREVFEQYDHMVGTD TVVPPGFGAAVMRIKRDGGYSLVTHSRADLALQDTYWGTL IAVLESVRKTLSVGAEPLAITNCVNYGDPDVDPVGLSAMM TALKNACEFSGVPVASGNASLYNTYQGKPIPPTLVVGMLG KVNPQKVAKPKPSKVFAVGWNDFELEREKELWRAIRKLSE EGAFILSSSQLLTRTHVETFREYGLKIEVKLPEVRPAHQM VLVFSERTPVVDVPVKEIGTLSR F:  MPLFKFAIDVQYRSNVRDPRGETIERVLREEKGLPVKKLR LGKSIHLEVEAENKEKAYEIVKKACEELLVNPVVEEYEVR EL G:  MPLFKFAIDVQYRSNVRDPRGETIERVLREEKGLPVKKLR LGKSIHLEVEAENKEKAYEIVKKACEELLVNPVVEEYEVR EL H:  MKPRACVVVYPGSNCDRDAYHALEINGFEPSYVGLDDKLD DYELIILPGGFSYGDYLRPGAVAAREKIAFEIAKAAERGK LIMGIXNGFQILIEMGLLKGALLQNSSGKFICKWVDLIVE NNDTPFTNAFEKGEKIRIPIAHGFGRYVKIDDVNVVLRYV KDVNGSDERIAGVLNESGNVFGLMPHPERAVEELIGGEDG KKVFQSILNYLK I:  KLRYLNILKEKLGREPTFVELQAFSVMWSEHCGYSHTKKY IRRLPKTGNAGVVNLDDYYSVAFKIESHNHPSAIEPYNGA ATGVGGIIRDVLAMGARPTAIFDSLHMSRIIDGIIEGIAD YGNSIGVPTVGGELRISSLYAHNPLVNVLAAGVVRNDMLV DSKASRPGQVIVIFGGATGRDGTKLSIQVGDPFAEKMLIE AFLEMVEEGLVEGAQDLGAGGVLSATSELVAKGNLGAIVH LDRVPLREPDMEPWEILISESQERMAVVTSPQKASRILEI ARKHLLFGDVVAEVIEEPVYRVMYRNDLVMEVPVQLLANA PEEDIVEYTPGKIPEFKRVEFEEVNAREVFEQYDHMVGTD TVVPPGFGAAVMRIKRDGGYSLVTHSRADLALQDTYWGTL IAVLESVRKTLSVGAEPLAITNCVNYGDPDVDPVGLSAMM TALKNACEFSGVPVASGNASLYNTYQGKPIPPTLVVGMLG KVNPQKVAKPKPSKVFAVGWNDFELEREKELWRAIRKLSE EGAFILSSSQLLTRTHVETFREYGLKIEVKLPEVRPAHQM VLVFSERTPVVDVPVKEIGTLSR J:  MPLFKFAIDVQYRSNVRDPRGETIERVLREEKGLPVKKLR LGKSIHLEVEAENKEKAYEIVKKACEELLVNPVVEEYEVR EL K:  MPLFKFAIDVQYRSNVRDPRGETIERVLREEKGLPVKKLR LGKSIHLEVEAENKEKAYEIVKKACEELLVNPVVEEYEVR EL L:  MKPRACVVVYPGSNCDRDAYHALEINGFEPSYVGLDDKLD DYELIILPGGFSYGDYLRPGAVAAREKIAFEIAKAAERGK LIMGIXNGFQILIEMGLLKGALLQNSSGKFICKWVDLIVE NNDTPFTNAFEKGEKIRIPIAHGFGRYVKIDDVNVVLRYV KDVNGSDERIAGVLNESGNVFGLMPHPERAVEELIGGEDG KKVFQSILNYLK 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 I residue 94 type sequence D description BINDING SITE FOR RESIDUE NA I 3001 source : AC2 4) chain I residue 236 type sequence D description BINDING SITE FOR RESIDUE NA I 3001 source : AC2 5) chain E residue 94 type sequence D description BINDING SITE FOR RESIDUE NA E 3002 source : AC3 6) chain E residue 236 type sequence D description BINDING SITE FOR RESIDUE NA E 3002 source : AC3 7) chain A residue 107 type sequence D description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 8) chain A residue 135 type sequence G description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 9) chain A residue 136 type sequence G description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 10) chain A residue 137 type sequence E description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 11) chain A residue 138 type sequence L description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 12) chain A residue 139 type sequence R description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 13) chain A residue 366 type sequence A description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 14) chain A residue 370 type sequence F description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 15) chain A residue 373 type sequence Y description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 16) chain A residue 385 type sequence P description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 17) chain A residue 386 type sequence G description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 18) chain A residue 388 type sequence G description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 19) chain A residue 429 type sequence K description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 20) chain A residue 548 type sequence S description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 21) chain A residue 553 type sequence T description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 22) chain A residue 555 type sequence T description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 23) chain A residue 556 type sequence H description BINDING SITE FOR RESIDUE ADP A 2004 source : AC4 24) chain I residue 107 type sequence D description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 25) chain I residue 135 type sequence G description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 26) chain I residue 136 type sequence G description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 27) chain I residue 137 type sequence E description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 28) chain I residue 138 type sequence L description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 29) chain I residue 139 type sequence R description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 30) chain I residue 366 type sequence A description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 31) chain I residue 370 type sequence F description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 32) chain I residue 373 type sequence Y description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 33) chain I residue 385 type sequence P description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 34) chain I residue 386 type sequence G description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 35) chain I residue 388 type sequence G description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 36) chain I residue 429 type sequence K description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 37) chain I residue 548 type sequence S description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 38) chain I residue 553 type sequence T description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 39) chain I residue 555 type sequence T description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 40) chain I residue 556 type sequence H description BINDING SITE FOR RESIDUE ADP I 2005 source : AC5 41) chain E residue 107 type sequence D description BINDING SITE FOR RESIDUE ADP E 2006 source : AC6 42) chain E residue 135 type sequence G description BINDING SITE FOR RESIDUE ADP E 2006 source : AC6 43) chain E residue 136 type sequence G description BINDING SITE FOR RESIDUE ADP E 2006 source : AC6 44) chain E residue 137 type sequence E description BINDING SITE FOR RESIDUE ADP E 2006 source : AC6 45) chain E residue 138 type sequence L description BINDING SITE FOR RESIDUE ADP E 2006 source : AC6 46) chain E residue 139 type sequence R description BINDING SITE FOR RESIDUE ADP E 2006 source : AC6 47) chain E residue 366 type sequence A description BINDING SITE FOR RESIDUE ADP E 2006 source : AC6 48) chain E residue 370 type sequence F description BINDING SITE FOR RESIDUE ADP E 2006 source : AC6 49) chain E residue 373 type sequence Y description BINDING SITE FOR RESIDUE ADP E 2006 source : AC6 50) chain E residue 385 type sequence P description BINDING SITE FOR RESIDUE ADP E 2006 source : AC6 51) chain E residue 386 type sequence G description BINDING SITE FOR RESIDUE ADP E 2006 source : AC6 52) chain E residue 388 type sequence G description BINDING SITE FOR RESIDUE ADP E 2006 source : AC6 53) chain E residue 429 type sequence K description BINDING SITE FOR RESIDUE ADP E 2006 source : AC6 54) chain E residue 548 type sequence S description BINDING SITE FOR RESIDUE ADP E 2006 source : AC6 55) chain E residue 553 type sequence T description BINDING SITE FOR RESIDUE ADP E 2006 source : AC6 56) chain E residue 555 type sequence T description BINDING SITE FOR RESIDUE ADP E 2006 source : AC6 57) chain E residue 556 type sequence H description BINDING SITE FOR RESIDUE ADP E 2006 source : AC6 58) chain A residue 35 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 source Swiss-Prot : SWS_FT_FI3 59) chain A residue 68 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 source Swiss-Prot : SWS_FT_FI3 60) chain A residue 442 type BINDING sequence N description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 source Swiss-Prot : SWS_FT_FI3 61) chain E residue 35 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 source Swiss-Prot : SWS_FT_FI3 62) chain E residue 68 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 source Swiss-Prot : SWS_FT_FI3 63) chain E residue 442 type BINDING sequence N description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 source Swiss-Prot : SWS_FT_FI3 64) chain I residue 35 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 source Swiss-Prot : SWS_FT_FI3 65) chain I residue 68 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 source Swiss-Prot : SWS_FT_FI3 66) chain I residue 442 type BINDING sequence N description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 source Swiss-Prot : SWS_FT_FI3 67) 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 68) 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 69) 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 70) 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 71) 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 72) 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 73) 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 74) chain E residue 70 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526 source Swiss-Prot : SWS_FT_FI4 75) chain E residue 94 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526 source Swiss-Prot : SWS_FT_FI4 76) chain E residue 236 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526 source Swiss-Prot : SWS_FT_FI4 77) chain E residue 478 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526 source Swiss-Prot : SWS_FT_FI4 78) 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 79) chain A residue 71 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI5 80) chain E residue 136 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI5 81) chain E residue 208 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI5 82) chain E residue 280 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI5 83) chain E residue 480 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI5 84) chain I residue 71 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI5 85) chain I residue 93 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI5 86) chain I residue 136 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI5 87) chain I residue 208 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI5 88) chain A residue 93 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI5 89) chain I residue 280 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI5 90) chain I residue 480 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI5 91) chain A residue 136 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI5 92) chain A residue 208 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI5 93) chain A residue 280 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI5 94) chain A residue 480 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI5 95) chain E residue 71 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI5 96) chain E residue 93 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI5 97) chain A residue 107 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 98) chain E residue 556 type BINDING sequence H description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 99) chain I residue 107 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 100) chain I residue 388 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 101) chain I residue 429 type BINDING sequence K description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 102) chain I residue 549 type BINDING sequence S description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 103) chain I residue 556 type BINDING sequence H description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 104) chain A residue 388 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 105) chain A residue 429 type BINDING sequence K description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 106) chain A residue 549 type BINDING sequence S description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 107) chain A residue 556 type BINDING sequence H description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 108) chain E residue 107 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 109) chain E residue 388 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 110) chain E residue 429 type BINDING sequence K description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 111) chain E residue 549 type BINDING sequence S description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 112) chain D residue 86 type ACT_SITE sequence X description Nucleophile => ECO:0000305|PubMed:18597481 source Swiss-Prot : SWS_FT_FI1 113) chain H residue 86 type ACT_SITE sequence X description Nucleophile => ECO:0000305|PubMed:18597481 source Swiss-Prot : SWS_FT_FI1 114) chain L residue 86 type ACT_SITE sequence X description Nucleophile => ECO:0000305|PubMed:18597481 source Swiss-Prot : SWS_FT_FI1 115) chain D residue 186 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:18597481 source Swiss-Prot : SWS_FT_FI2 116) chain D residue 188 type ACT_SITE sequence E description ACT_SITE => ECO:0000305|PubMed:18597481 source Swiss-Prot : SWS_FT_FI2 117) chain H residue 186 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:18597481 source Swiss-Prot : SWS_FT_FI2 118) chain H residue 188 type ACT_SITE sequence E description ACT_SITE => ECO:0000305|PubMed:18597481 source Swiss-Prot : SWS_FT_FI2 119) chain L residue 186 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:18597481 source Swiss-Prot : SWS_FT_FI2 120) chain L residue 188 type ACT_SITE sequence E description ACT_SITE => ECO:0000305|PubMed:18597481 source Swiss-Prot : SWS_FT_FI2 121) chain A residue 246-258 type prosite sequence TSELVAKGNLGAI description PTR2_2 PTR2 family proton/oligopeptide symporters signature 2. TseLVAkGNLGAI source prosite : PS01023 122) 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 123) chain E 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 124) 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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