eF-site ID 1dan-HLTU PDB Code 1dan Chain H, L, T, U click to enlarge Title Complex of active site inhibited human blood coagulation factor VIIA with human recombinant soluble tissue factor Classification HYDROLASE/HYDROLASE INHIBITOR Compound BLOOD COAGULATION FACTOR VIIA light chain Source (TF_HUMAN) Sequence H:  IVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAA HCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPS TYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERT LAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQ QSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHY RGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMR SEPRPGVLLRAPFP L:  ANAFLXXLRPGSLXRXCKXXQCSFXXARXIFKDAXRTKLF WISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRN CETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSL LADGVSCTPTVEYPCGKIPILE T:  TVAAYNLTWKSTNFKTILEWEPKPVNQVYTVQISTKSGDW KSKCFYTTDTECDLTDEIVKDVKQTYLARVFSYPA U:  EPLYENSPEFTPYLETNLGQPTIQSFEQVGTKVNVTVEDE RTLVRRNNTFLSLRDVFGKDLIYTLYYWSGKKTAKTNTNE FLIDVDKGENYCFSVQAVIPSRTVNRKSTDSPVECM Description (1)  BLOOD COAGULATION FACTOR VIIA, SOLUBLE TISSUE FACTOR, D-PHE-PHE-ARG-CHLOROMETHYLKETONE (DFFRCMK) WITH CHLOROMETHYLKETONE REPLACED BY A METHYLENE GROUP, METHYLENE GROUP Functional site 1) chain H residue 175 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:3264725 source Swiss-Prot : SWS_FT_FI3 2) chain L residue 7 type CARBOHYD sequence X description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:3264725 source Swiss-Prot : SWS_FT_FI3 3) chain L residue 14 type CARBOHYD sequence X description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:3264725 source Swiss-Prot : SWS_FT_FI3 4) chain L residue 16 type CARBOHYD sequence X description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:3264725 source Swiss-Prot : SWS_FT_FI3 5) chain L residue 20 type CARBOHYD sequence X description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:3264725 source Swiss-Prot : SWS_FT_FI3 6) chain L residue 25 type CARBOHYD sequence X description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:3264725 source Swiss-Prot : SWS_FT_FI3 7) chain L residue 26 type CARBOHYD sequence X description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:3264725 source Swiss-Prot : SWS_FT_FI3 8) chain L residue 29 type CARBOHYD sequence X description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:3264725 source Swiss-Prot : SWS_FT_FI3 9) chain L residue 35 type CARBOHYD sequence X description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:3264725 source Swiss-Prot : SWS_FT_FI3 10) chain L residue 63 type MOD_RES sequence D description (3R)-3-hydroxyaspartate => ECO:0000269|PubMed:3264725 source Swiss-Prot : SWS_FT_FI5 11) chain L residue 52 type CARBOHYD sequence S description O-linked (Xyl...) serine; alternate => ECO:0000269|PubMed:1904059, ECO:0000269|PubMed:2129367, ECO:0000269|PubMed:21949356, ECO:0000269|PubMed:2511201 source Swiss-Prot : SWS_FT_FI6 12) chain L residue 60 type CARBOHYD sequence S description O-linked (Fuc) serine => ECO:0000269|PubMed:1904059, ECO:0000269|PubMed:9023546 source Swiss-Prot : SWS_FT_FI7 13) chain T residue 45-62 type prosite sequence WKSKCFYTTDTECDLTDE description TISSUE_FACTOR Tissue factor signature. WKsKCfyTtDTECDLTDE source prosite : PS00621 14) chain H residue 53-58 type prosite sequence VSAAHC description TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC source prosite : PS00134 15) chain H residue 189-200 type prosite sequence DSCKGDSGGPHA description TRYPSIN_SER Serine proteases, trypsin family, serine active site. DSckGDSGGPHA source prosite : PS00135 16) chain L residue 61-72 type prosite sequence CKDQLQSYICFC description ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDqlqsYiCfC source prosite : PS00010 17) chain L residue 16-41 type prosite sequence XCKXXQCSFXXARXIFKDAXRTKLFW description GLA_1 Vitamin K-dependent carboxylation domain. EckEEqCsfeearEifkdaertkl.FW source prosite : PS00011 18) chain L residue 70-81 type prosite sequence CFCLPAFEGRNC description EGF_1 EGF-like domain signature 1. CfClpAfeGRnC source prosite : PS00022 19) chain L residue 112-127 type prosite sequence CRCHEGYSLLADGVSC description EGF_2 EGF-like domain signature 2. CrCheGYslladgvsC source prosite : PS01186 20) chain L residue 46-70 type prosite sequence DGDQCASSPCQNGGSCKDQLQSYIC description EGF_CA Calcium-binding EGF-like domain signature. DgDQCassp..........Cqnggs..CkDqlqsYiC source prosite : PS01187 21) chain H residue 189 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 22) chain U residue 124 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 23) chain U residue 137 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 24) chain H residue 195 type CARBOHYD sequence S description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 25) chain L residue 19 type MOD_RES sequence X description 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3264725 source Swiss-Prot : SWS_FT_FI4

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