4jcn

X-ray diffraction
1.8Å resolution

Structure of ESP, serine protease from Staphylococcus epidermidis

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142902 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamyl endopeptidase Chain: A
Molecule details ›
Chain: A
Length: 216 amino acids
Theoretical weight: 23.6 KDa
Source organism: Staphylococcus epidermidis ATCC 12228
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C0Q2 (Residues: 67-282; Coverage: 85%)
Gene names: SE_1543, esp, gseA
Sequence domains: Trypsin-like peptidase domain
Structure domains: Trypsin-like serine proteases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 39.41Å b: 60.36Å c: 42.34Å
α: 90° β: 98.59° γ: 90°
R-values:
R R work R free
0.175 0.173 0.199
Expression system: Escherichia coli