› 3o5b

X-ray diffraction
1.97Å resolution

Crystal structure of dimeric KlHxk1 in crystal form VII with glucose bound (open state)

Released:
DOI: 10.2210/pdb3o5b/pdb
PDB entry 3o5b coloured by chain, front view.
PDB entry 3o5b coloured by chain, side view.
PDB entry 3o5b coloured by chain, top view.
Source organism: Kluyveromyces lactis
Primary publication:
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 EB, Kettner K, Keim A, Svergun DI, Volke D, Singer D, Hoffmann R, Müller EC, Otto A, Kriegel TM, Sträter N
J Biol Chem 285 41019-33 (2010)
PMID: 20943665

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

2 bound ligands:
Ligand BGC 2 x BGC
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21212
Unit cell:
a: 98.14Å b: 122.2Å c: 92.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.204 0.255
Expression system: Kluyveromyces lactis

Quick links

Citations

1 review citation

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

4 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)
3 more