› 4k30

X-ray diffraction
2.1Å resolution

Structure of the N-acetyltransferase domain of human N-acetylglutamate synthase

Released:
DOI: 10.2210/pdb4k30/pdb
PDB entry 4k30 coloured by chain, front view.
PDB entry 4k30 coloured by chain, side view.
PDB entry 4k30 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the N-acetyltransferase domain of human N-acetyl-L-glutamate synthase in complex with N-acetyl-L-glutamate provides insights into its catalytic and regulatory mechanisms.
Zhao G, Jin Z, Allewell NM, Tuchman M, Shi D
PLoS One 8 e70369 (2013)
PMID: 23894642

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185354 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetylglutamate synthase conserved domain form Chains: A, B, X, Y
Molecule details ›
Chains: A, B, X, Y
Length: 160 amino acids
Theoretical weight: 18.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8N159 (Residues: 377-534; Coverage: 30%)
Gene name: NAGS
Sequence domains: NAT, N-acetyltransferase, of N-acetylglutamate synthase
Structure domains: Aminopeptidase

Ligands and Environments

1 bound ligand:
Ligand NLG 4 x NLG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P43212
Unit cell:
a: 116.141Å b: 116.141Å c: 109.742Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.185 0.244
Expression system: Escherichia coli

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Citations

4 review citations

Mitochondrial transport and metabolism of the vitamin B-derived cofactors thiamine pyrophosphate, coenzyme A, FAD and NAD+ , and related diseases: A review.
Palmieri et al. (2022)
3 more

5 mentions without citation

DNA Sliding Clamps as Therapeutic Targets.
Altieri et al. (2018)
4 more