› 2c0y

X-ray diffraction
2.1Å resolution

THE CRYSTAL STRUCTURE OF A CYS25ALA MUTANT OF HUMAN PROCATHEPSIN S

Released:
DOI: 10.2210/pdb2c0y/pdb
PDB entry 2c0y coloured by chain, front view.
PDB entry 2c0y coloured by chain, side view.
PDB entry 2c0y coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystal structure of a Cys25 -> Ala mutant of human procathepsin S elucidates enzyme-prosequence interactions.
Kaulmann G, Palm GJ, Schilling K, Hilgenfeld R, Wiederanders B
Protein Sci 15 2619-29 (2006)
PMID: 17075137

Function and Biology Details

Reaction catalysed: 
Similar to cathepsin L, but with much less activity on Z-Phe-Arg-|-NHMec, and more activity on the Z-Val-Val-Arg-|- compound.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150575 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathepsin S Chain: A
Molecule details ›
Chain: A
Length: 315 amino acids
Theoretical weight: 35.84 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P25774 (Residues: 17-331; Coverage: 100%)
Gene name: CTSS
Sequence domains:
Structure domains: Cysteine proteinases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: C2221
Unit cell:
a: 59.86Å b: 140.54Å c: 78.61Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.198 0.242
Expression system: Trichoplusia ni

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Citations

1 review citation

Specialized roles for cysteine cathepsins in health and disease.
Reiser et al. (2010)
8 other articles

3 mentions without citation

Mechanisms Applied by Protein Inhibitors to Inhibit Cysteine Proteases.
TuĊĦar et al. (2021)
2 more