3sbk

X-ray diffraction
2.55Å resolution

Russell's viper venom serine proteinase, RVV-V (PPACK-bound form)

Released:
Source organism: Daboia siamensis

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:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-148484 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P6522
Unit cell:
a: 77.233Å b: 77.233Å c: 168.433Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.25 0.246 0.328