› 2ch6

X-ray diffraction
2.72Å resolution

Crystal structure of human N-acetylglucosamine kinase in complex with ADP and glucose

Released:
DOI: 10.2210/pdb2ch6/pdb
PDB entry 2ch6 coloured by chain, front view.
PDB entry 2ch6 coloured by chain, side view.
PDB entry 2ch6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of human N-Acetylglucosamine kinase in two complexes with N-Acetylglucosamine and with ADP/glucose: insights into substrate specificity and regulation.
Weihofen WA, Berger M, Chen H, Saenger W, Hinderlich S
J Mol Biol 364 388-99 (2006)
PMID: 17010375

Function and Biology Details

Reactions catalysed: 
ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-D-glucosamine 6-phosphate
ATP + N-acyl-D-mannosamine = ADP + N-acyl-D-mannosamine 6-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193803 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetyl-D-glucosamine kinase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 344 amino acids
Theoretical weight: 37.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9UJ70 (Residues: 1-344; Coverage: 100%)
Gene name: NAGK
Sequence domains: BadF/BadG/BcrA/BcrD ATPase family
Structure domains: Nucleotidyltransferase; domain 5

Ligands and Environments

2 bound ligands:
Ligand ADP 4 x ADP
Ligand GLC 4 x GLC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21212
Unit cell:
a: 135.71Å b: 101.992Å c: 110.181Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.227 0.289
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Metabolic glycoengineering: sialic acid and beyond.
Du et al. (2009)
2 more

4 mentions without citation

Molecular modeling of the bifunctional enzyme UDP-GlcNAc 2-epimerase/ManNAc kinase and predictions of structural effects of mutations associated with HIBM and sialuria.
Kurochkina et al. (2010)
3 more