› 2pcu

X-ray diffraction
1.6Å resolution

Human carboxypeptidase A4 in complex with a cleaved hexapeptide.

Released:
DOI: 10.2210/pdb2pcu/pdb
PDB entry 2pcu coloured by chain, front view.
PDB entry 2pcu coloured by chain, side view.
PDB entry 2pcu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Caught after the Act: a human A-type metallocarboxypeptidase in a product complex with a cleaved hexapeptide.
Bayés A, Fernández D, Solà M, Marrero A, García-Piqué S, Avilés FX, Vendrell J, Gomis-Rüth FX
Biochemistry 46 6921-30 (2007)
PMID: 17506531

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163159 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Carboxypeptidase A4 Chain: A
Molecule details ›
Chain: A
Length: 305 amino acids
Theoretical weight: 34.23 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: Q9UI42 (Residues: 116-420; Coverage: 75%)
Gene names: CPA3, CPA4, UNQ694/PRO1339
Sequence domains: Zinc carboxypeptidase
Structure domains: Zn peptidases
peptide Chain: B
Molecule details ›
Chain: B
Length: 5 amino acids
Theoretical weight: 633 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

5 bound ligands:
Ligand NAG 1 x NAG
Ligand ZN 1 x ZN
Ligand SCN 1 x SCN
Ligand GOL 1 x GOL
Ligand ASP 1 x ASP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 50.304Å b: 72.494Å c: 81.575Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.159 0.176
Expression systems:
  • Komagataella pastoris
  • Not provided

Quick links

Citations

2 review citations

Structure and mechanism of metallocarboxypeptidases.
Gomis-Rüth FX. (2008)
1 more

5 mentions without citation

Proteome-derived peptide libraries to study the substrate specificity profiles of carboxypeptidases.
Tanco et al. (2013)
4 more