eF-site ID 1z6j-L PDB Code 1z6j Chain L click to enlarge Title Crystal Structure of a ternary complex of Factor VIIa/Tissue Factor/Pyrazinone Inhibitor Classification HYDROLASE Compound Coagulation factor VII Source (TF_HUMAN) Sequence L:  ANAFLXXLRPGSLXRXCKXXQCSFXXARXIFKDAXRTKLF WISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRN CETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSL LADGVSCTPTVEYPCGKIPILE Description (1)  Blood coagulation factor VIIa (E.C.3.4.21.21), Soluble tissue factor, Pyrazinone inhibitor with benzamidine as the P1 warhead Functional site 1) chain L residue 46 type sequence D description BINDING SITE FOR RESIDUE CA L 401 source : AC2 2) chain L residue 47 type sequence G description BINDING SITE FOR RESIDUE CA L 401 source : AC2 3) chain L residue 49 type sequence Q description BINDING SITE FOR RESIDUE CA L 401 source : AC2 4) chain L residue 63 type sequence D description BINDING SITE FOR RESIDUE CA L 401 source : AC2 5) chain L residue 64 type sequence Q description BINDING SITE FOR RESIDUE CA L 401 source : AC2 6) chain L residue 14 type sequence X description BINDING SITE FOR RESIDUE MG L 402 source : AC3 7) chain L residue 19 type sequence X description BINDING SITE FOR RESIDUE MG L 402 source : AC3 8) 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 9) 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 10) chain L residue 61-72 type prosite sequence CKDQLQSYICFC description ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDqlqsYiCfC source prosite : PS00010 11) chain L residue 16-41 type prosite sequence XCKXXQCSFXXARXIFKDAXRTKLFW description GLA_1 Vitamin K-dependent carboxylation domain. EckEEqCsfeearEifkdaertkl.FW source prosite : PS00011 12) chain L residue 70-81 type prosite sequence CFCLPAFEGRNC description EGF_1 EGF-like domain signature 1. CfClpAfeGRnC source prosite : PS00022 13) chain L residue 112-127 type prosite sequence CRCHEGYSLLADGVSC description EGF_2 EGF-like domain signature 2. CrCheGYslladgvsC source prosite : PS01186 14) chain L residue 46-70 type prosite sequence DGDQCASSPCQNGGSCKDQLQSYIC description EGF_CA Calcium-binding EGF-like domain signature. DgDQCassp..........Cqnggs..CkDqlqsYiC source prosite : PS01187 15) chain L residue 7 type BINDING sequence X description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 16) chain L residue 14 type BINDING sequence X description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 17) chain L residue 16 type BINDING sequence X description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 18) chain L residue 20 type BINDING sequence X description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 19) chain L residue 25 type BINDING sequence X description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 20) chain L residue 26 type BINDING sequence X description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 21) chain L residue 29 type BINDING sequence X description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 22) chain L residue 35 type BINDING sequence X description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 23) chain L residue 63 type MOD_RES sequence D description (3R)-3-hydroxyaspartate => ECO:0000269|PubMed:3264725 source Swiss-Prot : SWS_FT_FI4

Display surface Download Links