X-ray diffraction
2.9Å resolution

Crystal structure of a serine protease from Streptococcus pyogenes


Function and Biology Details

Reaction catalysed:
The primary cleavage site is at 67-His-|-Lys-68 in human C5a with a minor secondary cleavage site at 58-Ala-|-Ser-59
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
C5a peptidase Chain: A
Molecule details ›
Chain: A
Length: 1519 amino acids
Theoretical weight: 168.21 KDa
Source organism: Streptococcus pyogenes
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
  • Canonical: Q3HV58 (Residues: 34-1613; Coverage: 94%)
Gene name: scpC
Sequence domains:

Ligands and Environments

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P6222
Unit cell:
a: 191.969Å b: 191.969Å c: 252.788Å
α: 90° β: 90° γ: 120°
R R work R free
0.198 0.195 0.255
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'