PDBe 2o8l

X-ray diffraction
1.5Å resolution

Structure of V8 protease from staphylococcus aureus

Released:
Source organism: Staphylococcus aureus
Primary publication:
The structure of a universally employed enzyme: V8 protease from Staphylococcus aureus.
Acta Crystallogr. D Biol. Crystallogr. 60 256-9 (2004)
PMID: 14747701

Function and Biology Details

Reaction catalysed:
Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamyl endopeptidase Chain: A
Molecule details ›
Chain: A
Length: 274 amino acids
Theoretical weight: 29.68 KDa
Source organism: Staphylococcus aureus
UniProt:
  • Canonical: Q99V45 (Residues: 69-342; Coverage: 88%)
Gene names: SAV1048, sspA
Sequence domains: Trypsin-like peptidase domain
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P6522
Unit cell:
a: 59.43Å b: 59.43Å c: 214.01Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.188 0.219