› 2itm

X-ray diffraction
2.1Å resolution

Crystal structure of the E. coli xylulose kinase complexed with xylulose

Released:
DOI: 10.2210/pdb2itm/pdb
PDB entry 2itm coloured by chain, front view.
PDB entry 2itm coloured by chain, side view.
PDB entry 2itm coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural and kinetic studies of induced fit in xylulose kinase from Escherichia coli.
Di Luccio E, Petschacher B, Voegtli J, Chou HT, Stahlberg H, Nidetzky B, Wilson DK
J Mol Biol 365 783-98 (2007)
PMID: 17123542

Function and Biology Details

Reaction catalysed: 
ATP + D-xylulose = ADP + D-xylulose 5-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140552 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Xylulose kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 484 amino acids
Theoretical weight: 52.67 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P09099 (Residues: 1-484; Coverage: 100%)
Gene names: JW3536, b3564, xylB
Sequence domains:
Structure domains: Nucleotidyltransferase; domain 5

Ligands and Environments

3 bound ligands:
Ligand XUL 2 x XUL
Ligand SO4 2 x SO4
Ligand NH4 12 x NH4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P212121
Unit cell:
a: 61.883Å b: 112.605Å c: 143.073Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.201 0.263
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

7 mentions without citation

The sedoheptulose kinase CARKL directs macrophage polarization through control of glucose metabolism.
Haschemi et al. (2012)
6 more