› 7edd

X-ray diffraction
2.9Å resolution

Crystal structure of a serine protease from Streptococcus pyogenes

Released:
DOI: 10.2210/pdb7edd/pdb
PDB entry 7edd coloured by chain, front view.
PDB entry 7edd coloured by chain, side view.
PDB entry 7edd coloured by chain, top view.
Source organism: Streptococcus pyogenes
Primary publication:
The Autocatalytic Cleavage Domain Is Not Required for the Activity of ScpC, a Virulence Protease from Streptococcus pyogenes: A Structural Insight.
Jobichen C, Ying Chong T, Hui Ling T, Sivaraman J
Biochemistry 60 1564-1568 (2021)
PMID: 33929828

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:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174564 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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'
UniProt:
  • Canonical: Q3HV58 (Residues: 34-1613; Coverage: 94%)
Gene name: scpC
Sequence domains:

Ligands and Environments

6 bound ligands:
Ligand SO4 3 x SO4
Ligand CA 10 x CA
Ligand GOL 5 x GOL
Ligand MG 1 x MG
Ligand PEG 1 x PEG
Ligand CL 2 x CL
1 modified residue:
Ligand MSE 30 x MSE

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-values:
R R work R free
0.198 0.195 0.255
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

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