4jg3

X-ray diffraction
1.8Å resolution

Crystal structure of catabolite repression control protein (crc) from Pseudomonas aeruginosa

Released:

Function and Biology Details

Reaction catalysed:
Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-175925 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endonuclease/exonuclease/phosphatase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 262 amino acids
Theoretical weight: 30.1 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: Q51380 (Residues: 1-259; Coverage: 100%)
Gene names: ALP65_01013, CAZ10_32350, DT376_09125, GNQ48_25180, GUL26_21635, IPC1295_10410, IPC737_07685, NCTC13621_05232, PAERUG_P19_London_7_VIM_2_05_10_01808, crc, exoA
Sequence domains: Endonuclease/Exonuclease/phosphatase family
Structure domains: Endonuclease/exonuclease/phosphatase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P3221
Unit cell:
a: 74.659Å b: 74.659Å c: 123.161Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.194 0.22
Expression system: Escherichia coli