› 2h5m

Solution NMR

NMR Solution Structure of a GCN5-like putative N-acetyltransferase from Staphylococcus aureus complexed with acetyl-CoA. Northeast Structural Genomics Consortium Target ZR31

Released:
DOI: 10.2210/pdb2h5m/pdb
PDB entry 2h5m coloured by chain, ensemble of 20 models, front view.
PDB entry 2h5m coloured by chain, ensemble of 20 models, side view.
PDB entry 2h5m coloured by chain, ensemble of 20 models, top view.
Source organism: Staphylococcus aureus subsp. aureus COL
Primary publication:
Structure of an acetyl-CoA binding protein from Staphylococcus aureus representing a novel subfamily of GCN5-related N-acetyltransferase-like proteins.
Cort JR, Ramelot TA, Murray D, Acton TB, Ma LC, Xiao R, Montelione GT, Kennedy MA
J Struct Funct Genomics 9 7-20 (2008)
PMID: 18709443

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101615 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetyltransferase, GNAT family Chain: A
Molecule details ›
Chain: A
Length: 102 amino acids
Theoretical weight: 11.63 KDa
Source organism: Staphylococcus aureus subsp. aureus COL
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0H2WXG3 (Residues: 1-94; Coverage: 100%)
Gene name: SACOL2532
Sequence domains: GCN5-related N-acetyl-transferase
Structure domains: Aminopeptidase

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Refinement method: Refinement was conducted with HADDOCK. Starting structures were the 1R57 ensemble, which is the protein in the absence of ligand
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Catalysis by protein acetyltransferase Gcn5.
Albaugh et al. (2021)
6 other articles

2 mentions without citation

Advances in protein NMR provided by the NIGMS Protein Structure Initiative: impact on drug discovery.
Montelione et al. (2010)
1 more