PDBe 3s9c

X-ray diffraction
1.8Å resolution

Russell's viper venom serine proteinase, RVV-V in complex with the fragment (residues 1533-1546) of human factor V

Released:

Function and Biology Details

Reaction catalysed:
Fully activates human clotting factor V by a single cleavage at the 1545- Trp-Tyr-Leu-Arg-|-Ser-Asn-Asn-Gly-1552 bond. Cattle, but not rabbit, factor V is cleaved, and no other proteins of the clotting system are attacked. Esterase activity is observed on Bz-Arg-OEt and Tos-Arg-OMe, and amidase activity on Phe-pipecolyl-Arg-NHPhNO(2). 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Coagulation factor V light chain Chain: B
Molecule details ›
Chain: B
Length: 14 amino acids
Theoretical weight: 1.67 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P12259 (Residues: 1561-1574; Coverage: 1%)
Gene name: F5
Factor V activator RVV-V gamma Chain: A
Molecule details ›
Chain: A
Length: 234 amino acids
Theoretical weight: 25.96 KDa
Source organism: Daboia siamensis
UniProt:
  • Canonical: P18965 (Residues: 25-260; Coverage: 97%)
Structure domains: Trypsin-like serine proteases

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P61
Unit cell:
a: 101.2Å b: 101.2Å c: 44.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.183 0.183 0.218
Expression system: Not provided