Function and Biology Details
Reaction catalysed:
Similar to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure domains:
Structure analysis Details
Assemblies composition:
Assembly name:
PDBe Complex ID:
PDB-CPX-137529 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Cathepsin L heavy chain
Molecule details ›
Chains: A, C
Length: 175 amino acids
Theoretical weight: 19.1 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases
Length: 175 amino acids
Theoretical weight: 19.1 KDa
Source organism: Homo sapiens
UniProt:
- Canonical:
P07711 (Residues: 114-288; Coverage: 55%)
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases
Cathepsin L light chain
Molecule details ›
Chains: B, D
Length: 42 amino acids
Theoretical weight: 4.78 KDa
Source organism: Homo sapiens
UniProt:
Structure domains: Cysteine proteinases. Chain C
Length: 42 amino acids
Theoretical weight: 4.78 KDa
Source organism: Homo sapiens
UniProt:
- Canonical: P07711 (Residues: 292-333; Coverage: 13%)
Structure domains: Cysteine proteinases. Chain C
HLA class II histocompatibility antigen gamma chain
Molecule details ›
Chains: I, J
Length: 65 amino acids
Theoretical weight: 7.26 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Thyroglobulin type-1 repeat
Structure domains: Thyroglobulin type-1
Length: 65 amino acids
Theoretical weight: 7.26 KDa
Source organism: Homo sapiens
UniProt:
- Canonical: P04233 (Residues: 210-274; Coverage: 22%)
Sequence domains: Thyroglobulin type-1 repeat
Structure domains: Thyroglobulin type-1
