› 2bdl

X-ray diffraction
2Å resolution

Cathepsin K complexed with a pyrrolidine ketoamide-based inhibitor

Released:
DOI: 10.2210/pdb2bdl/pdb
PDB 2bdl coloured by chain and viewed from the front.
PDB 2bdl coloured by chain and viewed from the side.
PDB 2bdl coloured by chain and viewed from the top.
Source organism: Homo sapiens
Entry author: Shewchuk LM

Function and Biology Details

Reaction catalysed: 
Broad proteolytic activity. With small-molecule substrates and inhibitors, the major determinant of specificity is P2, which is preferably Leu, Met > Phe, and not Arg.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathepsin K Chain: A
Molecule details ›
Chain: A
Length: 215 amino acids
Theoretical weight: 23.52 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P43235 (Residues: 115-329; Coverage: 69%)
Gene names: CTSK, CTSO, CTSO2
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

1 bound ligand:
Ligand 4PR 1 x 4PR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 38.06Å b: 50.338Å c: 105.891Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.193 0.241
Expression system: Spodoptera frugiperda

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Citations

2 review citations

Biochemical properties and regulation of cathepsin K activity.
Lecaille et al. (2008)
1 more

1 mention without citation

The discovery of potent, selective, and reversible inhibitors of the house dust mite peptidase allergen Der p 1: an innovative approach to the treatment of allergic asthma.
Newton et al. (2014)