eF-site ID 1w0y-L PDB Code 1w0y Chain L click to enlarge Title tf7a_3771 complex Classification HYDROLASE Compound BLOOD COAGULATION FACTOR VIIA Source (TF_HUMAN) Sequence L:  ANAFLXXLRPGSLXRXCKXXQCSFXXARXIFKDAERTKLF WISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRN CETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSL LADGVSCTPTVEYPCGKIPILE Description Functional site 1) 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_FI6 2) 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_FI5 3) chain L residue 61-72 type prosite sequence CKDQLQSYICFC description ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDqlqsYiCfC source prosite : PS00010 4) chain L residue 16-41 type prosite sequence XCKXXQCSFXXARXIFKDAERTKLFW description GLA_1 Vitamin K-dependent carboxylation domain. EckEEqCsfeearEifkdaertkl.FW source prosite : PS00011 5) chain L residue 70-81 type prosite sequence CFCLPAFEGRNC description EGF_1 EGF-like domain signature 1. CfClpAfeGRnC source prosite : PS00022 6) chain L residue 112-127 type prosite sequence CRCHEGYSLLADGVSC description EGF_2 EGF-like domain signature 2. CrCheGYslladgvsC source prosite : PS01186 7) chain L residue 46-70 type prosite sequence DGDQCASSPCQNGGSCKDQLQSYIC description EGF_CA Calcium-binding EGF-like domain signature. DgDQCassp..........Cqnggs..CkDqlqsYiC source prosite : PS01187 8) chain L residue 6 type MOD_RES sequence X description 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3264725, ECO:0000269|PubMed:3486420 source Swiss-Prot : SWS_FT_FI2 9) chain L residue 7 type MOD_RES sequence X description 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3264725, ECO:0000269|PubMed:3486420 source Swiss-Prot : SWS_FT_FI2 10) chain L residue 14 type MOD_RES sequence X description 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3264725, ECO:0000269|PubMed:3486420 source Swiss-Prot : SWS_FT_FI2 11) chain L residue 16 type MOD_RES sequence X description 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3264725, ECO:0000269|PubMed:3486420 source Swiss-Prot : SWS_FT_FI2 12) chain L residue 20 type MOD_RES sequence X description 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3264725, ECO:0000269|PubMed:3486420 source Swiss-Prot : SWS_FT_FI2 13) chain L residue 25 type MOD_RES sequence X description 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3264725, ECO:0000269|PubMed:3486420 source Swiss-Prot : SWS_FT_FI2 14) chain L residue 26 type MOD_RES sequence X description 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3264725, ECO:0000269|PubMed:3486420 source Swiss-Prot : SWS_FT_FI2 15) chain L residue 29 type MOD_RES sequence X description 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3264725, ECO:0000269|PubMed:3486420 source Swiss-Prot : SWS_FT_FI2 16) chain L residue 35 type MOD_RES sequence E description 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3264725, ECO:0000269|PubMed:3486420 source Swiss-Prot : SWS_FT_FI2 17) 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_FI3 18) chain L residue 63 type MOD_RES sequence D description (3R)-3-hydroxyaspartate => ECO:0000269|PubMed:3264725 source Swiss-Prot : SWS_FT_FI4

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