› 1deu

X-ray diffraction
1.7Å resolution

CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN X: A CYSTEINE PROTEASE WITH THE PROREGION COVALENTLY LINKED TO THE ACTIVE SITE CYSTEINE

Released:
DOI: 10.2210/pdb1deu/pdb
PDB entry 1deu coloured by chain, front view.
PDB entry 1deu coloured by chain, side view.
PDB entry 1deu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human procathepsin X: a cysteine protease with the proregion covalently linked to the active site cysteine.
Sivaraman J, Nägler DK, Zhang R, Ménard R, Cygler M
J Mol Biol 295 939-51 (2000)
PMID: 10656802

Function and Biology Details

Reaction catalysed: 
Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-193667 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathepsin Z Chains: A, B
Molecule details ›
Chains: A, B
Length: 277 amino acids
Theoretical weight: 31.18 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: Q9UBR2 (Residues: 27-303; Coverage: 99%)
Gene name: CTSZ
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P3221
Unit cell:
a: 84.82Å b: 84.82Å c: 169.72Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.204 0.204 0.215

Quick links

Citations

8 review citations

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

8 mentions without citation

Cysteine Proteases: Modes of Activation and Future Prospects as Pharmacological Targets.
Verma et al. (2016)
7 more