› 2nck

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF MYXOCOCCUS XANTHUS NUCLEOSIDE DIPHOSPHATE KINASE AND ITS INTERACTION WITH A NUCLEOTIDE SUBSTRATE AT 2.0 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb2nck/pdb
PDB entry 2nck coloured by chain, front view.
PDB entry 2nck coloured by chain, side view.
PDB entry 2nck coloured by chain, top view.
Source organism: Myxococcus xanthus
Primary publication:
Crystal structure of Myxococcus xanthus nucleoside diphosphate kinase and its interaction with a nucleotide substrate at 2.0 A resolution.
Williams RL, Oren DA, Muñoz-Dorado J, Inouye S, Inouye M, Arnold E
J Mol Biol 234 1230-47 (1993)
PMID: 8263923

Function and Biology Details

Reaction catalysed: 
ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147286 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nucleoside diphosphate kinase Chains: L, R
Molecule details ›
Chains: L, R
Length: 144 amino acids
Theoretical weight: 16.03 KDa
Source organism: Myxococcus xanthus
Expression system: Not provided
UniProt:
  • Canonical: P15266 (Residues: 2-145; Coverage: 99%)
Gene name: ndk
Sequence domains: Nucleoside diphosphate kinase
Structure domains: Nucleoside diphosphate kinase-like domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43212
Unit cell:
a: 63.5Å b: 63.5Å c: 158Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.17 not available
Expression system: Not provided

Quick links

Citations

8 review citations

Nm23/nucleoside diphosphate kinase: toward a structural and biochemical understanding of its biological functions.
de la Rosa et al. (1995)
7 more

3 mentions without citation

Structure, Folding and Stability of Nucleoside Diphosphate Kinases.
Georgescauld et al. (2020)
2 more