PDBe 1fh0

X-ray diffraction
1.6Å resolution

CRYSTAL STRUCTURE OF HUMAN CATHEPSIN V COMPLEXED WITH AN IRREVERSIBLE VINYL SULFONE INHIBITOR

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of human cathepsin V.
Biochemistry 39 12543-51 (2000)
PMID: 11027133

Function and Biology Details

Reaction catalysed:
The recombinant enzyme hydrolyzes proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val- Arg-NHMec). 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathepsin L2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 221 amino acids
Theoretical weight: 24.04 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: O60911 (Residues: 114-334; Coverage: 70%)
Gene names: CATL2, CTSL2, CTSU, CTSV, UNQ268/PRO305
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P6422
Unit cell:
a: 104.7Å b: 104.7Å c: 179.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.197 0.211
Expression system: Saccharomyces cerevisiae