› 5avj

X-ray diffraction
1.45Å resolution

Crystal structure of proteinase K from Engyodontium album

Released:
DOI: 10.2210/pdb5avj/pdb
PDB entry 5avj coloured by chain, front view.
PDB entry 5avj coloured by chain, side view.
PDB entry 5avj coloured by chain, top view.
Source organism: Parengyodontium album
Primary publication:
Derivatization of Proteinase K with Heavy Atoms Enhances Its Thermal Stability.
Yazawa K, Sugahara M, Yutani K, Takehira M, Numata K
ACS Catalysis 6 3036-3046 (2016)

Function and Biology Details

Reaction catalysed: 
Hydrolysis of keratin, and of other proteins with subtilisin-like specificity. Hydrolyzes peptide amides.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139275 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Proteinase K Chain: A
Molecule details ›
Chain: A
Length: 279 amino acids
Theoretical weight: 28.96 KDa
Source organism: Parengyodontium album
UniProt:
  • Canonical: P06873 (Residues: 106-384; Coverage: 76%)
Gene name: PROK
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

3 bound ligands:
Ligand NO3 4 x NO3
Ligand GOL 1 x GOL
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P43212
Unit cell:
a: 67.549Å b: 67.549Å c: 107.083Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.163 0.184

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