eF-site ID 2hru-A PDB Code 2hru Chain A click to enlarge Title T. maritima PurL complexed with ADP Classification LIGASE Compound Phosphoribosylformylglycinamidine synthase II Source null (PURL_THEMA) Sequence A:  KLRYLNILKEKLGREPTFVELQAFSVMWSEHCGYSHTKKY IRRLPKTGFEGNAGVVNLDDYYSVAFKIESANHPSAIEPY NGAATGVGGIIRDVLAMGARPTAIFDSLHMSRIIDGIIEG IADYGNSIGVPTVGGELRISSLYAHNPLVNVLAAGVVRND MLVDSKASRPGQVIVIFGGATGRDGIVGDPFAEKMLIEAF LEMVEEGLVEGAQDLGAGGVLSATSELVAKGNLGAIVHLD RVPLREPDMEPWEILISESQERMAVVTSPQKASRILEIAR KHLLFGDVVAEVIEEPVYRVMYRNDLVMEVPVQLLANAPE EDIVEYTPGKIPEFKRVEFEEVNAREVFEQYDHMVGTDTV VPPGFGAAVMRIKRDGGYSLVTHSRADLALQDTYWGTLIA VLESVRKTLSVGAEPLAITNCVNYGDPDVDPVGLSAMMTA LKNACEFSGVPVASGNASLYNTYQGKPIPPTLVVGMLGKV NPQKVAKPKPSKVFAVGWNDFELEREKELWRAIRKLSEEG AFILSSSQLLTRTHVETFREYGLKIEVKLPEVRPAHQMVL VFSERTPVVDVPVKEIGTLSR Description Functional site 1) chain A residue 70 type sequence E description BINDING SITE FOR RESIDUE MG A 901 source : AC1 2) chain A residue 94 type sequence D description BINDING SITE FOR RESIDUE MG A 901 source : AC1 3) chain A residue 236 type sequence D description BINDING SITE FOR RESIDUE MG A 901 source : AC1 4) chain A residue 53 type sequence N description BINDING SITE FOR RESIDUE MG A 902 source : AC2 5) chain A residue 94 type sequence D description BINDING SITE FOR RESIDUE MG A 902 source : AC2 6) chain A residue 236 type sequence D description BINDING SITE FOR RESIDUE MG A 902 source : AC2 7) chain A residue 248 type sequence E description BINDING SITE FOR RESIDUE MG A 903 source : AC3 8) chain A residue 35 type sequence Y description BINDING SITE FOR RESIDUE ADP A 2005 source : AC4 9) chain A residue 42 type sequence I description BINDING SITE FOR RESIDUE ADP A 2005 source : AC4 10) chain A residue 51 type sequence E description BINDING SITE FOR RESIDUE ADP A 2005 source : AC4 11) chain A residue 52 type sequence G description BINDING SITE FOR RESIDUE ADP A 2005 source : AC4 12) chain A residue 53 type sequence N description BINDING SITE FOR RESIDUE ADP A 2005 source : AC4 13) chain A residue 68 type sequence K description BINDING SITE FOR RESIDUE ADP A 2005 source : AC4 14) chain A residue 70 type sequence E description BINDING SITE FOR RESIDUE ADP A 2005 source : AC4 15) chain A residue 94 type sequence D description BINDING SITE FOR RESIDUE ADP A 2005 source : AC4 16) chain A residue 442 type sequence N description BINDING SITE FOR RESIDUE ADP A 2005 source : AC4 17) chain A residue 474 type sequence V description BINDING SITE FOR RESIDUE ADP A 2005 source : AC4 18) chain A residue 476 type sequence S description BINDING SITE FOR RESIDUE ADP A 2005 source : AC4 19) chain A residue 477 type sequence G description BINDING SITE FOR RESIDUE ADP A 2005 source : AC4 20) chain A residue 478 type sequence N description BINDING SITE FOR RESIDUE ADP A 2005 source : AC4 21) chain A residue 72 type ACT_SITE sequence A description Proton acceptor => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 35 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 68 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 442 type BINDING sequence N description BINDING => ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 246-258 type prosite sequence TSELVAKGNLGAI description PTR2_2 PTR2 family proton/oligopeptide symporters signature 2. TseLVAkGNLGAI source prosite : PS01023 26) 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 27) 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 28) 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 29) 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 30) 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 31) chain A residue 71 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI5 32) chain A residue 93 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI5 33) chain A residue 136 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI5 34) chain A residue 280 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI5 35) chain A residue 480 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI5 36) chain A residue 107 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 37) chain A residue 388 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 38) chain A residue 429 type BINDING sequence K description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 39) chain A residue 549 type BINDING sequence S description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 40) chain A residue 556 type BINDING sequence H description BINDING => ECO:0000305|PubMed:17154526 source Swiss-Prot : SWS_FT_FI6 41) 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

Display surface Download Links