› 5hzz

X-ray diffraction
1.8Å resolution

Crystal structure of DR2231_E47A mutant in complex with dUMP and manganese

Released:
DOI: 10.2210/pdb5hzz/pdb
PDB entry 5hzz coloured by chain, front view.
PDB entry 5hzz coloured by chain, side view.
PDB entry 5hzz coloured by chain, top view.
Source organism: Deinococcus radiodurans R1
Primary publication:
Deinococcus radiodurans DR2231 is a two-metal-ion mechanism hydrolase with exclusive activity on dUTP.
Mota CS, Gonçalves AM, de Sanctis D
FEBS J 283 4274-4290 (2016)
PMID: 27739259

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193254 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
HAD superfamily Cof-like phosphohydrolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 149 amino acids
Theoretical weight: 16.2 KDa
Source organism: Deinococcus radiodurans R1
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9RS96 (Residues: 1-144; Coverage: 97%)
Gene name: DR_2231
Sequence domains: Phosphoribosyl-ATP pyrophosphohydrolase
Structure domains: putative ntp pyrophosphohydrolase like domain

Ligands and Environments

2 bound ligands:
Ligand MN 6 x MN
Ligand UMP 2 x UMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21212
Unit cell:
a: 150.452Å b: 77.893Å c: 52.597Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.163 0.207
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

Structural features and functional implications of proteins enabling the robustness of Deinococcus radiodurans.
Chen et al. (2020)
1 other article

1 mention without citation

Deinococcus radiodurans DR2231 is a two-metal-ion mechanism hydrolase with exclusive activity on dUTP.
Mota et al. (2016)