› 2vxk

X-ray diffraction
1.8Å resolution

Structural comparison between Aspergillus fumigatus and human GNA1

Released:
DOI: 10.2210/pdb2vxk/pdb
PDB entry 2vxk coloured by chain, front view.
PDB entry 2vxk coloured by chain, side view.
PDB entry 2vxk coloured by chain, top view.
Source organism: Aspergillus fumigatus
Primary publication:
Structural and kinetic differences between human and Aspergillus fumigatus D-glucosamine-6-phosphate N-acetyltransferase.
Hurtado-Guerrero R, Raimi OG, Min J, Zeng H, Vallius L, Shepherd S, Ibrahim AF, Wu H, Plotnikov AN, van Aalten DM
Biochem J 415 217-23 (2008)
PMID: 18601654

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-175807 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetyltransferase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 190 amino acids
Theoretical weight: 21.13 KDa
Source organism: Aspergillus fumigatus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q4WCU5 (Residues: 1-190; Coverage: 100%)
Gene name: AFUA_6G02460
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand COA 1 x COA
2 bound ligands:
Ligand 16G 1 x 16G
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: C2221
Unit cell:
a: 70.606Å b: 100.826Å c: 55.35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.178 0.218
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Potential Antifungal Targets Based on Glucose Metabolism Pathways of Candida albicans.
Chen et al. (2020)
13 other articles

4 mentions without citation

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