› 3t90

X-ray diffraction
1.5Å resolution

Crystal structure of glucosamine-6-phosphate N-acetyltransferase from Arabidopsis thaliana

Released:
DOI: 10.2210/pdb3t90/pdb
PDB entry 3t90 coloured by chain, front view.
PDB entry 3t90 coloured by chain, side view.
PDB entry 3t90 coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Crystal structure and functional characterization of a glucosamine-6-phosphate N-acetyltransferase from Arabidopsis thaliana.
Riegler H, Herter T, Grishkovskaya I, Lude A, Ryngajllo M, Bolger ME, Essigmann B, Usadel B
Biochem J 443 427-37 (2012)
PMID: 22329777

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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192276 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucosamine 6-phosphate N-acetyltransferase Chain: A
Molecule details ›
Chain: A
Length: 149 amino acids
Theoretical weight: 17.06 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9LFU9 (Residues: 1-149; Coverage: 100%)
Gene names: At5g15770, F14F8.150, GNA1
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments

2 bound ligands:
Ligand EPE 1 x EPE
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: C2
Unit cell:
a: 68.52Å b: 47.174Å c: 42.223Å
α: 90° β: 100.74° γ: 90°
R-values:
R R work R free
0.167 0.165 0.201
Expression system: Escherichia coli

Quick links

Citations

7 citation in other articles

N-acetylglucosamine-1-P uridylyltransferase 1 and 2 are required for gametogenesis and embryo development in Arabidopsis thaliana.
Chen et al. (2014)
6 more

1 mention without citation

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