› 7q8g

X-ray diffraction
2.06Å resolution

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
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-219140 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Cathepsin L2 Chains: AA, BA
Molecule details ›
Chains: AA, BA
Length: 222 amino acids
Theoretical weight: 24.15 KDa
Source organism: Homo sapiens
Expression system: Komagataella phaffii GS115
UniProt:
  • Canonical: O60911 (Residues: 113-334; Coverage: 70%)
Gene names: CATL2, CTSL2, CTSU, CTSV, UNQ268/PRO305
Sequence domains: Papain family cysteine protease
ALAASS Peptide Chain: PA
Molecule details ›
Chain: PA
Length: 6 amino acids
Theoretical weight: 519 Da
Source organism: synthetic construct
Expression system: Not provided
EYS Peptide Chain: PB

Ligands and Environments

3 bound ligands:
Ligand CL 2 x CL
Ligand MPD 2 x MPD
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P43212
Unit cell:
a: 94.03Å b: 94.03Å c: 125.68Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 0.207
Expression systems:
  • Komagataella phaffii GS115
  • Not provided

Quick links

Citations

3 citation in other articles

Calpeptin is a potent cathepsin inhibitor and drug candidate for SARS-CoV-2 infections.
Reinke et al. (2023)
2 more

1 mention without citation

Proteomic data and structure analysis combined reveal interplay of structural rigidity and flexibility on selectivity of cysteine cathepsins.
Tušar et al. (2023)

PDB-REDO

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