› 2ch5

X-ray diffraction
1.9Å resolution

Crystal structure of human N-acetylglucosamine kinase in complex with N-acetylglucosamine

Released:
DOI: 10.2210/pdb2ch5/pdb
PDB entry 2ch5 coloured by chain, front view.
PDB entry 2ch5 coloured by chain, side view.
PDB entry 2ch5 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: 347 amino acids
Theoretical weight: 37.79 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

3 bound ligands:
Ligand NAG 3 x NAG
Ligand GOL 5 x GOL
Ligand NDG 1 x NDG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P1
Unit cell:
a: 57.537Å b: 98.482Å c: 101.981Å
α: 63.43° β: 75.66° γ: 75.06°
R-values:
R R work R free
0.167 0.167 0.199
Expression system: Escherichia coli BL21(DE3)

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Citations

3 review citations

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

3 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)
2 more