› 2p5x

X-ray diffraction
2Å resolution

Crystal structure of Maf domain of human N-acetylserotonin O-methyltransferase-like protein

Released:
DOI: 10.2210/pdb2p5x/pdb
PDB entry 2p5x coloured by chain, front view.
PDB entry 2p5x coloured by chain, side view.
PDB entry 2p5x coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides.
Tchigvintsev A, Tchigvintsev D, Flick R, Popovic A, Dong A, Xu X, Brown G, Lu W, Wu H, Cui H, Dombrowski L, Joo JC, Beloglazova N, Min J, Savchenko A, Caudy AA, Rabinowitz JD, Murzin AG, Yakunin AF
Chem Biol 20 1386-98 (2013)
PMID: 24210219

Function and Biology Details

Reaction catalysed: 
A nucleoside triphosphate + H(2)O = a nucleotide + diphosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131982 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable bifunctional dTTP/UTP pyrophosphatase/methyltransferase protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 230 amino acids
Theoretical weight: 25.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O95671 (Residues: 10-239; Coverage: 37%)
Gene name: ASMTL
Sequence domains: Maf-like protein
Structure domains: Maf protein

Ligands and Environments

1 bound ligand:
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21212
Unit cell:
a: 84.802Å b: 116.983Å c: 51.471Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.198 0.253
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Preventive DNA repair by sanitizing the cellular (deoxy)nucleoside triphosphate pool.
Nagy et al. (2014)
9 other articles

4 mentions without citation

Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides.
Tchigvintsev et al. (2013)
3 more