1kuh

X-ray diffraction
1.6Å resolution

ZINC PROTEASE FROM STREPTOMYCES CAESPITOSUS

Released:

Function and Biology Details

Reaction catalysed:
Hydrolyzes proteins with a preference for Tyr or Phe in the P1' position. Has no action on amino-acid p-nitroanilides.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-157465 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Extracellular small neutral protease Chain: A
Molecule details ›
Chain: A
Length: 132 amino acids
Theoretical weight: 14.39 KDa
Source organism: Streptomyces caespitosus
UniProt:
  • Canonical: P56406 (Residues: 1-132; Coverage: 100%)
Gene name: snpA
Sequence domains: Streptomyces extracellular neutral proteinase (M7) family
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 55.21Å b: 55.27Å c: 37.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.164 0.225