› 1xc3

X-ray diffraction
2.1Å resolution

Structure of a Putative Fructokinase from Bacillus subtilis

Released:
DOI: 10.2210/pdb1xc3/pdb
PDB entry 1xc3 coloured by chain, front view.
PDB entry 1xc3 coloured by chain, side view.
PDB entry 1xc3 coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Structural studies of ROK fructokinase YdhR from Bacillus subtilis: insights into substrate binding and fructose specificity.
Nocek B, Stein AJ, Jedrzejczak R, Cuff ME, Li H, Volkart L, Joachimiak A
J Mol Biol 406 325-42 (2011)
PMID: 21185308

Function and Biology Details

Reaction catalysed: 
ATP + D-fructose = ADP + D-fructose 6-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-126484 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative fructokinase Chain: A
Molecule details ›
Chain: A
Length: 302 amino acids
Theoretical weight: 32.74 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: O05510 (Residues: 1-299; Coverage: 100%)
Gene names: BSU05860, gmuE, ydhR
Sequence domains: ROK family
Structure domains: Nucleotidyltransferase; domain 5

Ligands and Environments

3 bound ligands:
Ligand PT 2 x PT
Ligand ZN 1 x ZN
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P3121
Unit cell:
a: 112.66Å b: 112.66Å c: 75.087Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.181 0.18 0.203
Expression system: Escherichia coli

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Citations

2 review citations

Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.
Bräsen et al. (2014)
1 more

2 mentions without citation

Structural studies of ROK fructokinase YdhR from Bacillus subtilis: insights into substrate binding and fructose specificity.
Nocek et al. (2011)
1 more