PDBsum entry 1wtg

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protein ligands metals Protein-protein interface(s) links
Hydrolase/blood clotting PDB id
Protein chains
142 a.a. *
254 a.a. *
191 a.a. *
_CA ×9
Waters ×511
* Residue conservation analysis
PDB id:
Name: Hydrolase/blood clotting
Title: Human factor viia-tissue factor complexed with ethylsulfonamide-d-biphenylalanine-gln-p-aminobenzamidine
Structure: Coagulation factor vii. Chain: l. Fragment: factor vii light chain. Synonym: serum prothrombin conversion accelerator, spca, proconvertin, eptacog alfa. Engineered: yes. Coagulation factor vii. Chain: h. Fragment: factor vii heavy chain.
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell: cho. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Trimer (from PQS)
2.20Å     R-factor:   0.204     R-free:   0.251
Authors: S.Kadono,S.Sakamoto,Y.Kikuchi,M.Oh-Eda,N.Yabuta,K.Kitazawa, T.Yoshihashi,T.Suzuki,T.Koga,K.Hattori,T.Shiraishi,M.Kodama H.Haramura,Y.Ono,T.Esaki,H.Sato,Y.Watanabe,S.Itoh,M.Ohta, T.Kozono
Key ref: S.Kadono et al. (2005). Novel interactions of large P3 moiety and small P4 moiety in the binding of the peptide mimetic factor VIIa inhibitor. Biochem Biophys Res Commun, 326, 859-865. PubMed id: 15607748 DOI: 10.1016/j.bbrc.2004.11.108
23-Nov-04     Release date:   23-Nov-05    
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Protein chain
Pfam   ArchSchema ?
P08709  (FA7_HUMAN) -  Coagulation factor VII
466 a.a.
142 a.a.*
Protein chain
Pfam   ArchSchema ?
P08709  (FA7_HUMAN) -  Coagulation factor VII
466 a.a.
254 a.a.
Protein chain
Pfam   ArchSchema ?
P13726  (TF_HUMAN) -  Tissue factor
295 a.a.
191 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 10 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains L, H: E.C.  - Coagulation factor VIIa.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolyzes one Arg-|-Ile bond in factor X to form factor Xa.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   2 terms 
  Biological process     blood coagulation   2 terms 
  Biochemical function     catalytic activity     3 terms  


DOI no: 10.1016/j.bbrc.2004.11.108 Biochem Biophys Res Commun 326:859-865 (2005)
PubMed id: 15607748  
Novel interactions of large P3 moiety and small P4 moiety in the binding of the peptide mimetic factor VIIa inhibitor.
S.Kadono, A.Sakamoto, Y.Kikuchi, M.Oh-Eda, N.Yabuta, K.Yoshihashi, T.Kitazawa, T.Suzuki, T.Koga, K.Hattori, T.Shiraishi, M.Haramura, H.Kodama, Y.Ono, T.Esaki, H.Sato, Y.Watanabe, S.Itoh, M.Ohta, T.Kozono.
Selective factor VIIa-tissue factor complex (FVIIa/TF) inhibition is seen as a promising target for developing new anticoagulant drugs. A novel peptide mimetic factor VIIa inhibitor, ethylsulfonamide-d-biphenylalanine-Gln-p-aminobenzamidine, shows 100-fold selectivity against thrombin in spite of its large P3 moiety, unlike previously reported FVIIa/TF selective inhibitors. X-ray crystal structure analysis reveals that the large P3 moiety, d-biphenylalanine, and the small P4 moiety, ethylsulfonamide, make novel interactions with the 170-loop and Lys192 of FVIIa/TF, respectively, accompanying ligand-induced conformational changes of the 170-loop, Gln217, and Lys192. Structural comparisons of FVIIa with thrombin and amino acid sequence comparisons among coagulation serine proteases suggest that these interactions play an important role in achieving selective inhibition for FVIIa/TF.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20045964 T.Shiraishi, S.Kadono, M.Haramura, H.Kodama, Y.Ono, H.Iikura, T.Esaki, T.Koga, K.Hattori, Y.Watanabe, A.Sakamoto, K.Yoshihashi, T.Kitazawa, K.Esaki, M.Ohta, H.Sato, and T.Kozono (2010).
Design and synthesis of peptidomimetic factor VIIa inhibitors.
  Chem Pharm Bull (Tokyo), 58, 38-44.
PDB code: 2zzu
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