PDBe 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:

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. 

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
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