› 1by8

X-ray diffraction
2.6Å resolution

THE CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN K

Released:
DOI: 10.2210/pdb1by8/pdb
PDB entry 1by8 coloured by chain, front view.
PDB entry 1by8 coloured by chain, side view.
PDB entry 1by8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystal structure of human procathepsin K.
LaLonde JM, Zhao B, Janson CA, D'Alessio KJ, McQueney MS, Orsini MJ, Debouck CM, Smith WW
Biochemistry 38 862-9 (1999)
PMID: 9893980

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:
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: 314 amino acids
Theoretical weight: 35.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P43235 (Residues: 16-329; Coverage: 100%)
Gene names: CTSK, CTSO, CTSO2
Sequence domains:
Structure domains: Cysteine proteinases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: C2221
Unit cell:
a: 56.78Å b: 156.55Å c: 96.26Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.214 0.344
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Cysteine cathepsins: from structure, function and regulation to new frontiers.
Turk et al. (2012)
7 more

23 mentions without citation

Mechanisms Applied by Protein Inhibitors to Inhibit Cysteine Proteases.
TuĊĦar et al. (2021)
22 more