PDBe 2pq2

X-ray diffraction
1.82Å resolution

Structure of serine proteinase K complex with a highly flexible hydrophobic peptide at 1.8A resolution

Released:
Entry authors: Ethayathulla AS, Singh AK, Singh N, Sharma S, Sinha M, Somvanshi RK, Kaur P, Dey S, Srinivasan A, Singh TP

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
Structure domains: Rossmann fold
GALAG peptide Chain: B
Molecule details ›
Chain: B
Length: 5 amino acids
Theoretical weight: 387 Da
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P43212
Unit cell:
a: 68.314Å b: 68.314Å c: 108.418Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.168 0.207
Expression system: Not provided