› 5nhy

X-ray diffraction
1.72Å resolution

Function and Biology Details

Reaction catalysed: 
2-hydroxy-dATP + H(2)O = 2-hydroxy-dAMP + diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153202 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Oxidized purine nucleoside triphosphate hydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 159 amino acids
Theoretical weight: 18.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P36639 (Residues: 1-156; Coverage: 100%)
Gene names: MTH1, NUDT1
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase

Ligands and Environments

3 bound ligands:
Ligand 8XT 2 x 8XT
Ligand SO4 7 x SO4
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 59.528Å b: 66.709Å c: 82.075Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.22 0.262
Expression system: Escherichia coli

Quick links

Citations

4 review citations

DNA-encoded libraries - an efficient small molecule discovery technology for the biomedical sciences.
Kunig et al. (2018)
3 more

1 mention without citation

Discovery of Potent and Selective MTH1 Inhibitors for Oncology: Enabling Rapid Target (In)Validation.
Farand et al. (2020)