› 1yt5

X-ray diffraction
2.3Å resolution

Crystal structure of NAD kinase from Thermotoga maritima

Released:
DOI: 10.2210/pdb1yt5/pdb
PDB entry 1yt5 coloured by chain, front view.
PDB entry 1yt5 coloured by chain, side view.
PDB entry 1yt5 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Structure of a NAD kinase from Thermotoga maritima at 2.3 A resolution.
Oganesyan V, Huang C, Adams PD, Jancarik J, Yokota HA, Kim R, Kim SH
Acta Crystallogr Sect F Struct Biol Cryst Commun 61 640-6 (2005)
PMID: 16511117

Function and Biology Details

Reaction catalysed: 
ATP + NAD(+) = ADP + NADP(+)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-194865 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD kinase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 258 amino acids
Theoretical weight: 29.28 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: Q9X255 (Residues: 1-258; Coverage: 100%)
Gene names: NADK, TM_1733
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 18 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P21212
Unit cell:
a: 131.448Å b: 137.153Å c: 58.253Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.213 0.28
Expression system: Escherichia coli K-12

Quick links

Citations

1 review citation

The power to reduce: pyridine nucleotides--small molecules with a multitude of functions.
Pollak et al. (2007)
5 other articles

4 mentions without citation

Analysis of the Staphylococcus aureus DgkB structure reveals a common catalytic mechanism for the soluble diacylglycerol kinases.
Miller et al. (2008)
3 more