3dns

X-ray diffraction
2.1Å resolution

The N-terminal domain of Ribosomal-protein-alanine acetyltransferase from Clostridium acetobutylicum ATCC 824

Released:
Source organism: Clostridium acetobutylicum
Entry authors: Nocek B, Hendricks R, Cobb G, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + an N-terminal L-alanyl-[S5 protein of 30S ribosome] = CoA + an N-terminal N-acetyl-L-alanyl-[S5 protein of 30S ribosome]
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-188942 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
[ribosomal protein uS5]-alanine N-acetyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 135 amino acids
Theoretical weight: 16.12 KDa
Source organism: Clostridium acetobutylicum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q97MP0 (Residues: 1-132; Coverage: 42%)
Gene name: CA_C0152
Structure domains: Aminopeptidase

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P41212
Unit cell:
a: 59.619Å b: 59.619Å c: 196.448Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.197 0.246
Expression system: Escherichia coli