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:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assemblies composition:
Assembly name:
Cathepsin D light chain (preferred)
PDBe Complex ID:
PDB-CPX-139521 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cathepsin D light chain
Molecule details ›
Chains: A, C, E, G
Length: 97 amino acids
Theoretical weight: 10.69 KDa
Source organism: Homo sapiens
UniProt:
Structure domains: Acid Proteases
Length: 97 amino acids
Theoretical weight: 10.69 KDa
Source organism: Homo sapiens
UniProt:
- Canonical:
P07339 (Residues: 65-161; Coverage: 25%)
Structure domains: Acid Proteases
Cathepsin D heavy chain
Molecule details ›
Chains: B, D, F, H
Length: 241 amino acids
Theoretical weight: 26.27 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
Length: 241 amino acids
Theoretical weight: 26.27 KDa
Source organism: Homo sapiens
UniProt:
- Canonical: P07339 (Residues: 170-410; Coverage: 62%)
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
