› 1iry

Solution NMR

Solution structure of the hMTH1, a nucleotide pool sanitization enzyme

Released:
DOI: 10.2210/pdb1iry/pdb
PDB entry 1iry coloured by chain, ensemble of 30 models, front view.
PDB entry 1iry coloured by chain, ensemble of 30 models, side view.
PDB entry 1iry coloured by chain, ensemble of 30 models, top view.
Source organism: Homo sapiens
Primary publication:
Structure of human MTH1, a Nudix family hydrolase that selectively degrades oxidized purine nucleoside triphosphates.
Mishima M, Sakai Y, Itoh N, Kamiya H, Furuichi M, Takahashi M, Yamagata Y, Iwai S, Nakabeppu Y, Shirakawa M
J Biol Chem 279 33806-15 (2004)
PMID: 15133035

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 domain:

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 Chain: A
Molecule details ›
Chain: A
Length: 156 amino acids
Theoretical weight: 17.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P36639 (Residues: 1-156; Coverage: 100%)
Gene names: MTH1, NUDT1
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Oxidative damage in nucleic acids and Parkinson's disease.
Nakabeppu et al. (2007)
5 more

2 mentions without citation

The evolution of function within the Nudix homology clan.
Srouji et al. (2017)
1 more