› 3o8m

X-ray diffraction
1.42Å resolution

Crystal structure of monomeric KlHxk1 in crystal form XI with glucose bound (closed state)

Released:
DOI: 10.2210/pdb3o8m/pdb
PDB entry 3o8m coloured by chain, front view.
PDB entry 3o8m coloured by chain, side view.
PDB entry 3o8m 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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152570 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hexokinase Chain: A
Molecule details ›
Chain: A
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 GLC 1 x GLC
Ligand BGC 1 x BGC
Ligand CL 4 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P212121
Unit cell:
a: 64.575Å b: 75.599Å c: 103.857Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 0.216
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

5 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)
4 more