4oc6

X-ray diffraction
2.64Å resolution

Structure of Cathepsin D with inhibitor 2-bromo-N-[(2S,3S)-4-{[2-(2,4-dichlorophenyl)ethyl][3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propanoyl]amino}-3-hydroxy-1-(3-phenoxyphenyl)butan-2-yl]-4,5-dimethoxybenzamide

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.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Cathepsin D light chain Chain: A
Molecule details ›
Chain: A
Length: 103 amino acids
Theoretical weight: 11.27 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P07339 (Residues: 60-162; Coverage: 26%)
Gene names: CPSD, CTSD
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
Cathepsin D heavy chain Chain: B
Molecule details ›
Chain: B
Length: 243 amino acids
Theoretical weight: 26.54 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P07339 (Residues: 170-412; Coverage: 62%)
Gene names: CPSD, CTSD
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P6122
Unit cell:
a: 77.022Å b: 77.022Å c: 251.586Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.211 0.207 0.282
Expression system: Spodoptera frugiperda