› 4a37

X-ray diffraction
1.6Å resolution

Metallo-carboxypeptidase from Pseudomonas Aeruginosa

Released:
DOI: 10.2210/pdb4a37/pdb
PDB 4a37 coloured by chain and viewed from the front.
PDB 4a37 coloured by chain and viewed from the side.
PDB 4a37 coloured by chain and viewed from the top.
Source organism: Pseudomonas aeruginosa
Primary publication:
The novel structure of a cytosolic M14 metallocarboxypeptidase (CCP) from Pseudomonas aeruginosa: a model for mammalian CCPs.
Otero A, Rodríguez de la Vega M, Tanco S, Lorenzo J, Avilés FX, Reverter D
FASEB J. (2012)
PMID: 22645247

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase M14 carboxypeptidase A domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 388 amino acids
Theoretical weight: 44.45 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9I012 (Residues: 1-375; Coverage: 100%)
Gene name: PA2831
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P21
Unit cell:
a: 41.89Å b: 83.84Å c: 107.45Å
α: 90° β: 96.37° γ: 90°
R-values:
R R work R free
0.198 0.198 0.213
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

The Emerging Roles of Axonemal Glutamylation in Regulation of Cilia Architecture and Functions.
Yang et al. (2021)
1 more

2 mentions without citation

The cytosolic carboxypeptidases CCP2 and CCP3 catalyze posttranslational removal of acidic amino acids.
Tort et al. (2014)
1 more