eF-site ID 5wfq-NQR PDB Code 5wfq Chain N, Q, R click to enlarge Title Ligand-bound Ras:SOS:Ras complex Classification SIGNALING PROTEIN Compound GTPase HRas Source null (SOS1_HUMAN) Sequence N:  QMRLPSADVYRFAEPDSEENIIFEENMQGIPIIKAGTVIK LIERLTYHMYADPNFVRTFLTTYRSFCKPQELLSLIIERF EIPEPEPTEADRIAIENGDQPLSAELKRFRKEYIQPVQLR VLNVCRHWVEHHFYDFERDAYLLQRMEEFIGTVRGKAMKK WVESITKIIQRKKIANITFQSSPPTVEWHISRPGHIETFD LLTLHPIEIARQLTLLESDLYRAVQPSELVGSVWTKEDKE INSPNLLKMIRHTTNLTLWFEKCIVETENLEERVAVVSRI IEILQVFQELNNFNGVLEVVSAMNSSPVYRLDHTFEQIPS RQKKILEEAHELSEDHYKKYLAKLRSINPPCVPFFGIYLT NILKTEEGNPEVLKRHGKELINFSKRRKVAEITGEIQQYQ NQPYCLRVESDIKRFFENLNPMGNSMEKEFTDYLFNKSLE IEPRNPKPLPRFPKKYSYPLKSPGVRPSNPR Q:  MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSY RKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLC VFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDL AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLV REIRQH R:  GMTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDS YRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFL CVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCD LAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTL VREIRQH Description Functional site 1) chain Q residue 17 type sequence S description binding site for residue MG Q 201 source : AC1 2) chain Q residue 35 type sequence T description binding site for residue MG Q 201 source : AC1 3) chain Q residue 12 type sequence G description binding site for residue GNP Q 202 source : AC2 4) chain Q residue 13 type sequence G description binding site for residue GNP Q 202 source : AC2 5) chain Q residue 14 type sequence V description binding site for residue GNP Q 202 source : AC2 6) chain Q residue 15 type sequence G description binding site for residue GNP Q 202 source : AC2 7) chain Q residue 16 type sequence K description binding site for residue GNP Q 202 source : AC2 8) chain Q residue 17 type sequence S description binding site for residue GNP Q 202 source : AC2 9) chain Q residue 18 type sequence A description binding site for residue GNP Q 202 source : AC2 10) chain Q residue 28 type sequence F description binding site for residue GNP Q 202 source : AC2 11) chain Q residue 29 type sequence V description binding site for residue GNP Q 202 source : AC2 12) chain Q residue 30 type sequence D description binding site for residue GNP Q 202 source : AC2 13) chain Q residue 31 type sequence E description binding site for residue GNP Q 202 source : AC2 14) chain Q residue 32 type sequence Y description binding site for residue GNP Q 202 source : AC2 15) chain Q residue 34 type sequence P description binding site for residue GNP Q 202 source : AC2 16) chain Q residue 35 type sequence T description binding site for residue GNP Q 202 source : AC2 17) chain Q residue 60 type sequence G description binding site for residue GNP Q 202 source : AC2 18) chain Q residue 61 type sequence Q description binding site for residue GNP Q 202 source : AC2 19) chain Q residue 116 type sequence N description binding site for residue GNP Q 202 source : AC2 20) chain Q residue 117 type sequence K description binding site for residue GNP Q 202 source : AC2 21) chain Q residue 119 type sequence D description binding site for residue GNP Q 202 source : AC2 22) chain Q residue 120 type sequence L description binding site for residue GNP Q 202 source : AC2 23) chain Q residue 145 type sequence S description binding site for residue GNP Q 202 source : AC2 24) chain Q residue 146 type sequence A description binding site for residue GNP Q 202 source : AC2 25) chain Q residue 147 type sequence K description binding site for residue GNP Q 202 source : AC2 26) chain N residue 852 type sequence V description binding site for residue 5UV N 1101 source : AC3 27) chain N residue 878 type sequence M description binding site for residue 5UV N 1101 source : AC3 28) chain N residue 879 type sequence N description binding site for residue 5UV N 1101 source : AC3 29) chain N residue 883 type sequence V description binding site for residue 5UV N 1101 source : AC3 30) chain N residue 884 type sequence Y description binding site for residue 5UV N 1101 source : AC3 31) chain N residue 886 type sequence L description binding site for residue 5UV N 1101 source : AC3 32) chain N residue 887 type sequence D description binding site for residue 5UV N 1101 source : AC3 33) chain N residue 890 type sequence F description binding site for residue 5UV N 1101 source : AC3 34) chain N residue 902 type sequence E description binding site for residue 5UV N 1101 source : AC3 35) chain N residue 927-960 type prosite sequence VPFFGIYLTNILKTEEGNPEVLKRHGKELINFSK description RASGEF Ras Guanine-nucleotide exchange factors domain signature. VPFfGiyLtNIlkteegnpevlkrhgkel.................INFsK source prosite : PS00720 36) chain Q residue 13 type BINDING sequence G description BINDING => ECO:0000269|PubMed:16698776 source Swiss-Prot : SWS_FT_FI1 37) chain R residue 145 type BINDING sequence S description BINDING => ECO:0000269|PubMed:16698776 source Swiss-Prot : SWS_FT_FI1 38) chain Q residue 29 type BINDING sequence V description BINDING => ECO:0000269|PubMed:16698776 source Swiss-Prot : SWS_FT_FI1 39) chain Q residue 59 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16698776 source Swiss-Prot : SWS_FT_FI1 40) chain Q residue 116 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16698776 source Swiss-Prot : SWS_FT_FI1 41) chain Q residue 145 type BINDING sequence S description BINDING => ECO:0000269|PubMed:16698776 source Swiss-Prot : SWS_FT_FI1 42) chain R residue 13 type BINDING sequence G description BINDING => ECO:0000269|PubMed:16698776 source Swiss-Prot : SWS_FT_FI1 43) chain R residue 29 type BINDING sequence V description BINDING => ECO:0000269|PubMed:16698776 source Swiss-Prot : SWS_FT_FI1 44) chain R residue 59 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16698776 source Swiss-Prot : SWS_FT_FI1 45) chain R residue 116 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16698776 source Swiss-Prot : SWS_FT_FI1 46) chain Q residue 1 type MOD_RES sequence M description N-acetylmethionine; in GTPase HRas; alternate => ECO:0000269|Ref.12 source Swiss-Prot : SWS_FT_FI2 47) chain R residue 1 type MOD_RES sequence M description N-acetylmethionine; in GTPase HRas; alternate => ECO:0000269|Ref.12 source Swiss-Prot : SWS_FT_FI2 48) chain Q residue 2 type MOD_RES sequence T description N-acetylthreonine; in GTPase HRas, N-terminally processed => ECO:0000269|Ref.12 source Swiss-Prot : SWS_FT_FI3 49) chain R residue 2 type MOD_RES sequence T description N-acetylthreonine; in GTPase HRas, N-terminally processed => ECO:0000269|Ref.12 source Swiss-Prot : SWS_FT_FI3 50) chain Q residue 118 type MOD_RES sequence C description S-nitrosocysteine => ECO:0000269|PubMed:9020151 source Swiss-Prot : SWS_FT_FI4 51) chain R residue 118 type MOD_RES sequence C description S-nitrosocysteine => ECO:0000269|PubMed:9020151 source Swiss-Prot : SWS_FT_FI4 52) chain Q residue 35 type CARBOHYD sequence T description (Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL => ECO:0000269|PubMed:19744486, ECO:0000269|PubMed:8626575, ECO:0000269|PubMed:8626586, ECO:0000269|PubMed:9632667 source Swiss-Prot : SWS_FT_FI5 53) chain R residue 35 type CARBOHYD sequence T description (Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL => ECO:0000269|PubMed:19744486, ECO:0000269|PubMed:8626575, ECO:0000269|PubMed:8626586, ECO:0000269|PubMed:9632667 source Swiss-Prot : SWS_FT_FI5

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