PDBe 1lya

X-ray diffraction
2.5Å resolution

CRYSTAL STRUCTURES OF NATIVE AND INHIBITED FORMS OF HUMAN CATHEPSIN D: IMPLICATIONS FOR LYSOSOMAL TARGETING AND DRUG DESIGN

Released:

Function and Biology Details

Reaction catalysed:
Specificity similar to, but narrower than, that of pepsin A. Does not cleave the 4-Gln-|-His-5 bond in B chain of insulin. 
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cathepsin D light chain Chains: A, C
Molecule details ›
Chains: A, C
Length: 97 amino acids
Theoretical weight: 10.69 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P07339 (Residues: 65-161; Coverage: 25%)
Gene names: CPSD, CTSD
Structure domains: Acid Proteases
Cathepsin D heavy chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 241 amino acids
Theoretical weight: 26.27 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P07339 (Residues: 170-410; Coverage: 62%)
Gene names: CPSD, CTSD
Structure domains: Acid Proteases

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P65
Unit cell:
a: 125.9Å b: 125.9Å c: 104.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.188 not available