› 1f3y

Solution NMR

SOLUTION STRUCTURE OF THE NUDIX ENZYME DIADENOSINE TETRAPHOSPHATE HYDROLASE FROM LUPINUS ANGUSTIFOLIUS L.

Released:
DOI: 10.2210/pdb1f3y/pdb
PDB entry 1f3y coloured by chain, ensemble of 25 models, front view.
PDB entry 1f3y coloured by chain, ensemble of 25 models, side view.
PDB entry 1f3y coloured by chain, ensemble of 25 models, top view.
Source organism: Lupinus angustifolius
Primary publication:
The three-dimensional structure of the Nudix enzyme diadenosine tetraphosphate hydrolase from Lupinus angustifolius L.
Swarbrick JD, Bashtannyk T, Maksel D, Zhang XR, Blackburn GM, Gayler KR, Gooley PR
J Mol Biol 302 1165-77 (2000)
PMID: 11183782

Function and Biology Details

Reaction catalysed: 
P(1),P(4)-bis(5'-guanosyl) tetraphosphate + H(2)O = GTP + GMP
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126454 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nudix hydrolase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 165 amino acids
Theoretical weight: 18.83 KDa
Source organism: Lupinus angustifolius
Expression system: Escherichia coli
UniProt:
  • Canonical: O04841 (Residues: 35-199; Coverage: 83%)
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: torsion angle dynamics,simulated annealing
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Structures and mechanisms of Nudix hydrolases.
Mildvan et al. (2005)
23 other articles

7 mentions without citation

Predicting data quality in biological X-ray solution scattering.
Wang et al. (2018)
6 more