› 2e2n

X-ray diffraction
1.9Å resolution

Crystal structure of Sulfolobus tokodaii hexokinase in the apo form

Released:
DOI: 10.2210/pdb2e2n/pdb
PDB entry 2e2n coloured by chain, front view.
PDB entry 2e2n coloured by chain, side view.
PDB entry 2e2n coloured by chain, top view.
Source organism: Sulfurisphaera tokodaii
Primary publication:
Crystal structures of an ATP-dependent hexokinase with broad substrate specificity from the hyperthermophilic archaeon Sulfolobus tokodaii.
Nishimasu H, Fushinobu S, Shoun H, Wakagi T
J Biol Chem 282 9923-9931 (2007)
PMID: 17229727

Function and Biology Details

Reaction catalysed: 
ATP + D-hexose = ADP + D-hexose 6-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-188786 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATPase BadF/BadG/BcrA/BcrD type domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 299 amino acids
Theoretical weight: 32.16 KDa
Source organism: Sulfurisphaera tokodaii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96Y14 (Residues: 1-299; Coverage: 100%)
Gene names: ST2354, STK_23540
Sequence domains: BadF/BadG/BcrA/BcrD ATPase family
Structure domains: Nucleotidyltransferase; domain 5

Ligands and Environments

2 bound ligands:
Ligand SO4 3 x SO4
Ligand EPE 1 x EPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P21
Unit cell:
a: 82.897Å b: 50.184Å c: 83.269Å
α: 90° β: 114.69° γ: 90°
R-values:
R R work R free
0.175 0.175 0.21
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Cohesion group approach for evolutionary analysis of TyrA, a protein family with wide-ranging substrate specificities.
Bonner et al. (2008)
1 more

8 mentions without citation

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