› 4n1u

X-ray diffraction
1.6Å 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: 158 amino acids
Theoretical weight: 18.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P36639 (Residues: 1-155; Coverage: 99%)
Gene names: MTH1, NUDT1
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase

Ligands and Environments

2 bound ligands:
Ligand 2GE 2 x 2GE
Ligand SO4 12 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P212121
Unit cell:
a: 57.658Å b: 66.073Å c: 72.477Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.18 0.204
Expression system: Escherichia coli

Quick links

Citations

64 review citations

Replication stress and cancer.
Gaillard et al. (2015)
63 more

3 mentions without citation

MTH1 Substrate Recognition--An Example of Specific Promiscuity.
Nissink et al. (2016)
2 more