› 2pjb

X-ray diffraction
1.7Å resolution

CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B 2-(3-Aminomethyl-phenyl)-3-{[1-((S)-2-benzyloxycarbonylamino-3-phenyl-propane-1-sulfonylamino)-2-methyl-propyl]-hydroxy-phosphinoyl}-propionic acid COMPLEX

Released:
DOI: 10.2210/pdb2pjb/pdb
PDB entry 2pjb coloured by chain, front view.
PDB entry 2pjb coloured by chain, side view.
PDB entry 2pjb coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Structures of potent selective peptide mimetics bound to carboxypeptidase B.
Adler M, Buckman B, Bryant J, Chang Z, Chu K, Emayan K, Hrvatin P, Islam I, Morser J, Sukovich D, West C, Yuan S, Whitlow M
Acta Crystallogr D Biol Crystallogr 64 149-57 (2008)
PMID: 18219114

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140836 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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

Ligands and Environments

2 bound ligands:
Ligand ZN 3 x ZN
Ligand 983 3 x 983
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 66.392Å b: 96.152Å c: 135.528Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.174 0.2

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Citations

5 review citations

Carboxypeptidase U (TAFIa): a new drug target for fibrinolytic therapy?
Willemse et al. (2009)
4 more