› 3fgu

X-ray diffraction
2.15Å resolution

Catalytic complex of Human Glucokinase

Released:
DOI: 10.2210/pdb3fgu/pdb
PDB entry 3fgu coloured by chain, front view.
PDB entry 3fgu coloured by chain, side view.
PDB entry 3fgu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The active conformation of human glucokinase is not altered by allosteric activators.
Petit P, Antoine M, Ferry G, Boutin JA, Lagarde A, Gluais L, Vincentelli R, Vuillard L
Acta Crystallogr D Biol Crystallogr 67 929-35 (2011)
PMID: 22101819

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-152941 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hexokinase-4 Chain: A
Molecule details ›
Chain: A
Length: 470 amino acids
Theoretical weight: 53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P35557 (Residues: 12-465; Coverage: 98%)
Gene name: GCK
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand BGC 1 x BGC
Ligand ANP 1 x ANP
Ligand MG 1 x MG
Ligand K 1 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 65.88Å b: 82.12Å c: 86.83Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.197 0.255
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Essential role of conformational selection in ligand binding.
Vogt et al. (2014)
2 more

7 mentions without citation

Solution NMR Spectroscopy for the Study of Enzyme Allostery.
Lisi et al. (2016)
6 more