PDBe 3gt3

X-ray diffraction
1.5Å resolution

Structure of proteinase K with the mad triangle B3C

Released:
Source organism: Parengyodontium album
Primary publication:
The magic triangle goes MAD: experimental phasing with a bromine derivative.
OpenAccess logo Acta Crystallogr. D Biol. Crystallogr. 66 374-80 (2010)
PMID: 20382990

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

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: 28.96 KDa
Source organism: Parengyodontium album
UniProt:
  • Canonical: P06873 (Residues: 106-384; Coverage: 76%)
Gene name: PROK
Sequence domains: Subtilase family
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P43212
Unit cell:
a: 67.84Å b: 67.84Å c: 101.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.145 0.143 0.184