PDBe 4zar

X-ray diffraction
1.15Å resolution

Crystal Structure of Proteinase K from Engyodontium albuminhibited by METHOXYSUCCINYL-ALA-ALA-PRO-PHE-CHLOROMETHYL KETONE at 1.15 A resolution

Released:
Entry authors: Sawaya MR, Cascio D, Collazo M, Bond C, Cohen A, DeNicola A, Eden K, Jain K, Leung C, Lubock N, McCormick J, Rosinski J, Spiegelman L, Athar Y, Tibrewal N, Winter J, Solomon S

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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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
METHOXYSUCCINYL-ALA-ALA-PRO-PHE-CHLOROMETHYL KETONE, bound form Chain: B
Molecule details ›
Chain: B
Length: 5 amino acids
Theoretical weight: 551 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P43212
Unit cell:
a: 67.85Å b: 67.85Å c: 102.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.112 0.11 0.134
Expression system: Not provided