› 3cxp

X-ray diffraction
2.01Å resolution

Crystal structure of human glucosamine 6-phosphate N-acetyltransferase 1 mutant E156A

Released:
DOI: 10.2210/pdb3cxp/pdb
PDB entry 3cxp coloured by chain, front view.
PDB entry 3cxp coloured by chain, side view.
PDB entry 3cxp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Acceptor substrate binding revealed by crystal structure of human glucosamine-6-phosphate N-acetyltransferase 1.
Wang J, Liu X, Liang YH, Li LF, Su XD
FEBS Lett 582 2973-8 (2008)
PMID: 18675810

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-188459 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucosamine 6-phosphate N-acetyltransferase Chain: A
Molecule details ›
Chain: A
Length: 184 amino acids
Theoretical weight: 20.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96EK6 (Residues: 1-184; Coverage: 100%)
Gene names: GNA1, GNPNAT1
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments

1 bound ligand:
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BSRF BEAMLINE 3W1A
Spacegroup: P43212
Unit cell:
a: 51.34Å b: 51.34Å c: 142.61Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.199 0.232
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Liver glucose metabolism in humans.
Adeva-Andany et al. (2016)
3 more

5 mentions without citation

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