› 2pkc

X-ray diffraction
1.5Å resolution

CRYSTAL STRUCTURE OF CALCIUM-FREE PROTEINASE K AT 1.5 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb2pkc/pdb
PDB entry 2pkc coloured by chain, front view.
PDB entry 2pkc coloured by chain, side view.
PDB entry 2pkc coloured by chain, top view.
Source organism: Parengyodontium album
Primary publication:
Crystal structure of calcium-free proteinase K at 1.5-A resolution.
Müller A, Hinrichs W, Wolf WM, Saenger W
J Biol Chem 269 23108-11 (1994)
PMID: 8083213

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Proteinase K Chain: A
Molecule details ›
Chain: A
Length: 279 amino acids
Theoretical weight: 28.93 KDa
Source organism: Parengyodontium album
Expression system: Not provided
UniProt:
  • Canonical: P06873 (Residues: 106-384; Coverage: 76%)
Gene name: PROK
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

1 bound ligand:
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43212
Unit cell:
a: 68.27Å b: 68.27Å c: 108.08Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 not available not available
Expression system: Not provided

Quick links

Citations

3 review citations

Surfomics: shaving live organisms for a fast proteomic identification of surface proteins.
Olaya-Abril et al. (2014)
2 more

1 mention without citation

High-resolution structure of proteinase K cocrystallized with digalacturonic acid.
Larson et al. (2009)