X-ray diffraction
2.02Å resolution

Function and Biology Details

Reaction catalysed:
Preferential release of a C-terminal lysine or arginine amino acid.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Carboxypeptidase B Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 306 amino acids
Theoretical weight: 34.74 KDa
Source organism: Sus scrofa
  • Canonical: P09955 (Residues: 111-416; Coverage: 76%)
Gene names: CPB, CPB1
Sequence domains: Zinc carboxypeptidase
Structure domains: Zn peptidases
Anabaenopeptin B Chains: F, G, H
Molecule details ›
Chains: F, G, H
Length: 6 amino acids
Theoretical weight: 855 Da
Source organism: Planktothrix rubescens

Ligands and Environments

1 bound ligand:
4 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P32
Unit cell:
a: 124.78Å b: 124.78Å c: 48.9Å
α: 90° β: 90° γ: 120°
R R work R free
0.176 0.176 0.229