› 3de5

X-ray diffraction
2.1Å resolution

roteinase K by Classical hanging drop method after the second step of high X-Ray dose on ESRF ID23-1 beamline

Released:
DOI: 10.2210/pdb3de5/pdb
PDB entry 3de5 coloured by chain, front view.
PDB entry 3de5 coloured by chain, side view.
PDB entry 3de5 coloured by chain, top view.
Source organism: Parengyodontium album
Primary publication:
Radiation stability of proteinase K crystals grown by LB nanotemplate method.
Pechkova E, Tripathi S, Ravelli RB, McSweeney S, Nicolini C
J Struct Biol 168 409-18 (2009)
PMID: 19686853

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: X
Molecule details ›
Chain: X
Length: 279 amino acids
Theoretical weight: 28.93 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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P43212
Unit cell:
a: 67.858Å b: 67.858Å c: 102.681Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.168 0.234

Quick links

Citations

1 review citation

Matrices for Sensors from Inorganic, Organic, and Biological Nanocomposites.
Nicolini et al. (2011)
8 other articles

1 mention without citation

Avoidable errors in deposited macromolecular structures: an impediment to efficient data mining.
Dauter et al. (2014)