› 1nqc

X-ray diffraction
1.8Å resolution

Crystal structures of Cathepsin S inhibitor complexes

Released:
DOI: 10.2210/pdb1nqc/pdb
PDB entry 1nqc coloured by chain, front view.
PDB entry 1nqc coloured by chain, side view.
PDB entry 1nqc coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Specificity determinants of human cathepsin s revealed by crystal structures of complexes.
Pauly TA, Sulea T, Ammirati M, Sivaraman J, Danley DE, Griffor MC, Kamath AV, Wang IK, Laird ER, Seddon AP, Ménard R, Cygler M, Rath VL
Biochemistry 42 3203-13 (2003)
PMID: 12641451

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:
  • not assigned
Sequence domains:
Structure domain:

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: 217 amino acids
Theoretical weight: 24.02 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P25774 (Residues: 115-331; Coverage: 69%)
Gene name: CTSS
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

1 bound ligand:
Ligand C4P 1 x C4P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P212121
Unit cell:
a: 36.9Å b: 76.5Å c: 101.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.199 0.219

Quick links

Citations

6 review citations

Cathepsin S inhibitors: 2004-2010.
Lee-Dutra et al. (2011)
5 more

7 mentions without citation

Cysteine cathepsin activity regulation by glycosaminoglycans.
Novinec et al. (2014)
6 more