› 1rkd

X-ray diffraction
1.84Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + D-ribose = ADP + D-ribose 5-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141890 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribokinase Chain: A
Molecule details ›
Chain: A
Length: 309 amino acids
Theoretical weight: 32.32 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A9J6 (Residues: 1-309; Coverage: 100%)
Gene names: JW3731, b3752, rbsK
Sequence domains: pfkB family carbohydrate kinase
Structure domains: UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase

Ligands and Environments

3 bound ligands:
Ligand RIB 1 x RIB
Ligand PO4 2 x PO4
Ligand ADP 1 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P6122
Unit cell:
a: 95.4Å b: 95.4Å c: 154.87Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.221 0.22 0.258
Expression system: Escherichia coli

Quick links

Citations

4 review citations

The structural and biochemical foundations of thiamin biosynthesis.
Jurgenson et al. (2009)
3 more

13 mentions without citation

Plant Fructokinases: Evolutionary, Developmental, and Metabolic Aspects in Sink Tissues.
Stein et al. (2018)
12 more