› 3o1w

X-ray diffraction
1.66Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + D-hexose = ADP + D-hexose 6-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152571 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hexokinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 485 amino acids
Theoretical weight: 53.67 KDa
Source organism: Kluyveromyces lactis
Expression system: Kluyveromyces lactis
UniProt:
  • Canonical: P33284 (Residues: 1-485; Coverage: 100%)
Gene names: KLLA0D11352g, RAG5
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand GOL 3 x GOL
Ligand NHE 4 x NHE
Ligand PO4 6 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.3
Spacegroup: P21
Unit cell:
a: 60.311Å b: 135.844Å c: 72.591Å
α: 90° β: 92.06° γ: 90°
R-values:
R R work R free
0.162 0.161 0.201
Expression system: Kluyveromyces lactis

Quick links

Citations

1 review citation

Moonlighting Proteins: The Case of the Hexokinases.
Rodríguez-Saavedra et al. (2021)
20 other articles

3 mentions without citation

Crystal structure of hexokinase KlHxk1 of Kluyveromyces lactis: a molecular basis for understanding the control of yeast hexokinase functions via covalent modification and oligomerization.
Kuettner et al. (2010)
2 more