› 4hvy

X-ray diffraction
1.46Å resolution

A thermostable variant of human NUDT18 NUDIX domain obtained by Hot Colony Filtration

Released:
DOI: 10.2210/pdb4hvy/pdb
PDB entry 4hvy coloured by chain, front view.
PDB entry 4hvy coloured by chain, side view.
PDB entry 4hvy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Engineering protein thermostability using a generic activity-independent biophysical screen inside the cell.
Asial I, Cheng YX, Engman H, Dollhopf M, Wu B, Nordlund P, Cornvik T
Nat Commun 4 2901 (2013)
PMID: 24352381

Function and Biology Details

Reaction catalysed: 
8-oxo-GDP + H(2)O = 8-oxo-GMP + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-180606 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
8-oxo-dGDP phosphatase NUDT18 Chain: A
Molecule details ›
Chain: A
Length: 162 amino acids
Theoretical weight: 18.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6ZVK8 (Residues: 26-179; Coverage: 48%)
Gene names: MTH3, NUDT18
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase

Ligands and Environments

4 bound ligands:
Ligand GOL 2 x GOL
Ligand MG 3 x MG
Ligand SO4 1 x SO4
Ligand NA 4 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: I4122
Unit cell:
a: 90.2Å b: 90.2Å c: 75.03Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.166 0.21
Expression system: Escherichia coli

Quick links

Citations

13 review citations

The Cellular Thermal Shift Assay: A Novel Biophysical Assay for In Situ Drug Target Engagement and Mechanistic Biomarker Studies.
Martinez Molina et al. (2016)
12 more

1 mention without citation

Nudix hydrolase 18 catalyzes the hydrolysis of active triphosphate metabolites of the antivirals remdesivir, ribavirin, and molnupiravir.
Jemth et al. (2022)