› 5lrg

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:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140837 (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
UniProt:
  • 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:
Ligand ZN 3 x ZN
4 modified residues:
Ligand 73N 3 x 73N
Ligand DLY 3 x DLY
Ligand 73O 3 x 73O
Ligand MAA 3 x MAA

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-values:
R R work R free
0.176 0.176 0.229

Quick links

Citations

3 review citations

Structural Biology and Protein Engineering of Thrombolytics.
Mican et al. (2019)
2 more

1 mention without citation

Isolation, Co-Crystallization and Structure-Based Characterization of Anabaenopeptins as Highly Potent Inhibitors of Activated Thrombin Activatable Fibrinolysis Inhibitor (TAFIa).
Schreuder et al. (2016)