› 1un9

X-ray diffraction
3.1Å resolution

Crystal structure of the dihydroxyacetone kinase from C. freundii in complex with AMP-PNP and Mg2+

Released:
DOI: 10.2210/pdb1un9/pdb
PDB entry 1un9 coloured by chain, front view.
PDB entry 1un9 coloured by chain, side view.
PDB entry 1un9 coloured by chain, top view.
Source organism: Citrobacter freundii
Primary publication:
Crystal structure of the Citrobacter freundii dihydroxyacetone kinase reveals an eight-stranded alpha-helical barrel ATP-binding domain.
Siebold C, Arnold I, Garcia-Alles LF, Baumann U, Erni B
J Biol Chem 278 48236-44 (2003)
PMID: 12966101

Function and Biology Details

Reaction catalysed: 
ATP + glycerone = ADP + glycerone phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155305 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydroxyacetone kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 552 amino acids
Theoretical weight: 57.85 KDa
Source organism: Citrobacter freundii
Expression system: Escherichia coli
UniProt:
  • Canonical: P45510 (Residues: 1-552; Coverage: 100%)
Gene name: dhaK
Sequence domains:
Structure domains: Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat

Ligands and Environments

3 bound ligands:
Ligand ANP 2 x ANP
Ligand MG 4 x MG
Ligand 2HA 2 x 2HA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.5
Spacegroup: C2221
Unit cell:
a: 100.788Å b: 124.869Å c: 236.53Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.237 0.237 not available
Expression system: Escherichia coli

Quick links

Citations

2 review citations

How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria.
Deutscher et al. (2006)
1 more

5 mentions without citation

A comprehensive update of the sequence and structure classification of kinases.
Cheek et al. (2005)
4 more