› 1vhg

X-ray diffraction
2.7Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155351 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ADP compounds hydrolase NudE Chains: A, B
Molecule details ›
Chains: A, B
Length: 198 amino acids
Theoretical weight: 22.86 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P45799 (Residues: 2-186; Coverage: 100%)
Gene names: JW3360, b3397, nudE, yrfE
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 14 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: I4132
Unit cell:
a: 193.168Å b: 193.168Å c: 193.168Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.211 0.272
Expression system: Escherichia coli

Quick links

Citations

23 review citations

Regulation of fatty acid metabolism in bacteria.
Fujita et al. (2007)
22 more

1 mention without citation

Nudix hydrolases degrade protein-conjugated ADP-ribose.
Daniels et al. (2015)