› 5hx1

X-ray diffraction
1.8Å resolution

Crystal structure of DR2231_E46A mutant in complex with dUMP and magnesium

Released:
DOI: 10.2210/pdb5hx1/pdb
PDB 5hx1 coloured by chain and viewed from the front.
PDB 5hx1 coloured by chain and viewed from the side.
PDB 5hx1 coloured by chain and viewed from the top.
Source organism: Deinococcus radiodurans
Primary publication:
Deinococcus radiodurans DR2231 is a two-metal-ion mechanism hydrolase with exclusive activity on dUTP.
Mota CS, Gon��alves AM, de Sanctis D
FEBS J. (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)
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: 138 amino acids
Theoretical weight: 14.97 KDa
Source organism: Deinococcus radiodurans
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9RS96 (Residues: 7-144; Coverage: 93%)
Gene name: DR_2231
Sequence domains: Phosphoribosyl-ATP pyrophosphohydrolase
Structure domains: putative ntp pyrophosphohydrolase like domain

Ligands and Environments

2 bound ligands:
Ligand UMP 2 x UMP
Ligand MG 4 x MG
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: 77.813Å c: 52.266Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.173 0.213
Expression system: Escherichia coli BL21

Quick links