PDBsum entry 2fjq

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protein links
Hydrolase PDB id
Protein chain
235 a.a.
Theoretical model
PDB id:
Name: Hydrolase
Title: Three dimensional model of the snake venom factor v activator from daboia lebetina
Structure: Factor v-activating enzyme precursor. Chain: a. Synonym: fva. Ec: 3.4.21.-
Source: Vipera lebetina. Elephant snake. Other_details: snake venom
Authors: K.Segers,J.Rosing,G.A.Nicolaes
Key ref:
K.Segers et al. (2006). Structural models of the snake venom factor V activators from Daboia russelli and Daboia lebetina. Proteins, 64, 968-984. PubMed id: 16807918 DOI: 10.1002/prot.21051
03-Jan-06     Release date:   11-Jul-06    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q9PT41  (VSPF5_MACLB) -  Factor V activator
259 a.a.
235 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: E.C.3.4.21.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]


DOI no: 10.1002/prot.21051 Proteins 64:968-984 (2006)
PubMed id: 16807918  
Structural models of the snake venom factor V activators from Daboia russelli and Daboia lebetina.
K.Segers, J.Rosing, G.A.Nicolaes.
Blood coagulation factor V (FV) is a multifunctional protein that circulates in human plasma as a precursor molecule which can be activated by thrombin or activated factor X (FXa) in order to express its cofactor activity in prothrombin activation. FV activation is achieved by limited proteolysis after Arg709, Arg1018, and Arg1545 in the FV molecule. The venoms of Daboia russelli and Daboia lebetina contain a serine protease that specifically activates FV by a single cleavage at Arg1545. We have predicted the three-dimensional structure of these enzymes using comparative protein modeling techniques. The plasminogen activator from Agkistrodon acutus, which shows a high degree of homology with the venom FV activators and for which a high-quality crystallographic structure is available, was used as the molecular template. The RVV-V and LVV-V models provide for the first time a detailed and accurate structure of a snake venom FV activator and explain the observed sensitivity or resistance toward a number of serine protease inhibitors. Finally, electrostatic potential calculations show that two positively charged surface patches are present on opposite sides of the active site. We propose that both FV activators achieve their exquisite substrate specificity for the Arg1545 site via interactions between these exosites and FV.
  Selected figure(s)  
Figure 1.
Figure 1. Activation of human FV by thrombin and the snake venom FV activators RVV-V and LVV-V. Thrombin-catalyzed FV activation proceeds via three sequential cleavages at Arg709, Arg1018, and Arg1545. The resulting activated FV molecule (FVa) is a heterodimeric protein consisting of a light chain doublet (71/74 kDa) and a heavy chain (105 kDa). The snake venom FV activators from Daboia russelli and Daboia lebetina cleave FV at Arg1545, giving rise to a FVa molecule with a light chain of 71/74 kDa and a heavy chain of around 290 kDa.
Figure 7.
Figure 7. Multiple sequence alignment of RVV-V, LVV-V, thrombin, and factor Xa. Residues are numbered using the chymotrypsinogen numbering scheme.[64] Loops surrounding the active site are indicated and boxed. The alignment was created using the ICM program (Molsoft LLC).
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2006, 64, 968-984) copyright 2006.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21277886 T.Sajevic, A.Leonardi, and I.Kri┼żaj (2011).
Haemostatically active proteins in snake venoms.
  Toxicon, 57, 627-645.  
17878169 K.Segers, B.Dahlbäck, P.E.Bock, G.Tans, J.Rosing, and G.A.Nicolaes (2007).
The role of thrombin exosites I and II in the activation of human coagulation factor V.
  J Biol Chem, 282, 33915-33924.  
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