› 5hva

X-ray diffraction
2.1Å resolution

Crystal structure of DR2231 in complex with dUMPNPP and magnesium.

Released:
DOI: 10.2210/pdb5hva/pdb
PDB entry 5hva coloured by chain, front view.
PDB entry 5hva coloured by chain, side view.
PDB entry 5hva coloured by chain, top view.
Source organism: Deinococcus radiodurans
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: 140 amino acids
Theoretical weight: 15.23 KDa
Source organism: Deinococcus radiodurans
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9RS96 (Residues: 5-144; Coverage: 95%)
Gene name: DR_2231
Sequence domains: Phosphoribosyl-ATP pyrophosphohydrolase
Structure domains: putative ntp pyrophosphohydrolase like domain

Ligands and Environments

2 bound ligands:
Ligand MG 6 x MG
Ligand DUP 2 x DUP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21212
Unit cell:
a: 148.827Å b: 77.841Å c: 52.56Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.177 0.233
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

2 mentions without citation

Structural basis of G-quadruplex unfolding by the DEAH/RHA helicase DHX36.
Chen et al. (2018)
1 more