PDBe 5isv

X-ray diffraction
1.35Å resolution

Crystal structure of the ribosomal-protein-S18-alanine N-acetyltransferase from Escherichia coli

Released:
Source organism: Escherichia coli O157:H7
Entry authors: Filippova EV, Minasov G, Kiryukhina O, Shuvalova L, Grimshaw S, Wolfe AJ, Anderson WF, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + an N-terminal L-alanyl-[S18 protein of 30S ribosome] = CoA + an N-terminal N-acetyl-L-alanyl-[S18 protein of 30S ribosome]
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribosomal-protein-alanine acetyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 165 amino acids
Theoretical weight: 18.59 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A946 (Residues: 1-148; Coverage: 100%)
Gene names: ECs5331, Z5974, rimI
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P1
Unit cell:
a: 40.222Å b: 41.785Å c: 46.404Å
α: 93.74° β: 90.08° γ: 116.52°
R-values:
R R work R free
0.158 0.156 0.209
Expression system: Escherichia coli BL21(DE3)