› 4ag7

X-ray diffraction
1.55Å resolution

C. elegans glucosamine-6-phosphate N-acetyltransferase (GNA1): coenzyme A adduct

Released:
DOI: 10.2210/pdb4ag7/pdb
PDB entry 4ag7 coloured by chain, front view.
PDB entry 4ag7 coloured by chain, side view.
PDB entry 4ag7 coloured by chain, top view.
Source organism: Caenorhabditis elegans
Primary publication:
Structural and biochemical characterization of a trapped coenzyme A adduct of Caenorhabditis elegans glucosamine-6-phosphate N-acetyltransferase 1.
Dorfmueller HC, Fang W, Rao FV, Blair DE, Attrill H, van Aalten DM
Acta Crystallogr D Biol Crystallogr 68 1019-29 (2012)
PMID: 22868768

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + D-glucosamine 6-phosphate = CoA + N-acetyl-D-glucosamine 6-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172635 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucosamine 6-phosphate N-acetyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 165 amino acids
Theoretical weight: 18.48 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q17427 (Residues: 1-165; Coverage: 100%)
Gene names: B0024.12, gna-1
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand COA 2 x COA
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P61
Unit cell:
a: 86.072Å b: 86.072Å c: 77.285Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.178 0.214
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 citation in other articles

Inference of Functionally-Relevant N-acetyltransferase Residues Based on Statistical Correlations.
Neuwald et al. (2016)
8 more

3 mentions without citation

Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT).
Salah Ud-Din et al. (2016)
2 more