› 4ag9

X-ray diffraction
1.76Å resolution

C. elegans glucosamine-6-phosphate N-acetyltransferase (GNA1): ternary complex with coenzyme A and GlcNAc

Released:
DOI: 10.2210/pdb4ag9/pdb
Model geometry
Fit model/data
PDB entry 4ag9 coloured by chain, front view.
PDB entry 4ag9 coloured by chain, side view.
PDB entry 4ag9 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
OpenAccess logo 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
2 bound ligands:
Ligand EDO 2 x EDO
Ligand 16G 2 x 16G
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P212121
Unit cell:
a: 48.872Å b: 53.353Å c: 135.096Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.19 0.232
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 citation in other articles

Combinatorial pathway enzyme engineering and host engineering overcomes pyruvate overflow and enhances overproduction of N-acetylglucosamine in Bacillus subtilis.
Ma et al. (2019)
6 more

6 mentions without citation

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