› 4jhc

X-ray diffraction
1.85Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141518 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
7-methyl-GTP pyrophosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 215 amino acids
Theoretical weight: 24.15 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A729 (Residues: 1-194; Coverage: 100%)
Gene names: JW5155, b1087, yceF
Sequence domains: Maf-like protein
Structure domains: Maf protein

Ligands and Environments

2 bound ligands:
Ligand GOL 3 x GOL
Ligand UNX 12 x UNX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P212121
Unit cell:
a: 50.413Å b: 52.856Å c: 128.948Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.194 0.247
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

2 mentions without citation

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