› 2bdl

X-ray diffraction
2Å resolution

Cathepsin K complexed with a pyrrolidine ketoamide-based inhibitor

Released:
DOI: 10.2210/pdb2bdl/pdb
PDB entry 2bdl coloured by chain, front view.
PDB entry 2bdl coloured by chain, side view.
PDB entry 2bdl coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Novel, potent P2-P3 pyrrolidine derivatives of ketoamide-based cathepsin K inhibitors.
Barrett DG, Catalano JG, Deaton DN, Hassell AM, Long ST, Miller AB, Miller LR, Ray JA, Samano V, Shewchuk LM, Wells-Knecht KJ, Willard DH, Wright LL
Bioorg Med Chem Lett 16 1735-9 (2006)
PMID: 16376075

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:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154996 (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

Quick links

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)