› 1obr

X-ray diffraction
2.3Å resolution

Function and Biology Details

Reaction catalysed: 
Releases a C-terminal residue, which may be hydrophobic or positively charged.
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-151339 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carboxypeptidase T Chain: A
Molecule details ›
Chain: A
Length: 326 amino acids
Theoretical weight: 36.96 KDa
Source organism: Thermoactinomyces vulgaris
UniProt:
  • Canonical: P29068 (Residues: 99-424; Coverage: 81%)
Gene name: cpt
Sequence domains: Zinc carboxypeptidase
Structure domains: Zn peptidases

Ligands and Environments

3 bound ligands:
Ligand ZN 1 x ZN
Ligand CA 4 x CA
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OTHER
Spacegroup: P6322
Unit cell:
a: 159.42Å b: 159.42Å c: 106.86Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.152 0.152 not available

Quick links

Citations

3 review citations

Bacterial protease inhibitors.
Supuran et al. (2002)
2 more

7 mentions without citation

A network representation of protein structures: implications for protein stability.
Brinda et al. (2005)
6 more