2i79

X-ray diffraction
2.1Å resolution

The crystal structure of the acetyltransferase of GNAT family from Streptococcus pneumoniae

Released:
Entry authors: Zhang RG, Zhou M, Abdullah J, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetyltransferase domain-containing protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 172 amino acids
Theoretical weight: 19.36 KDa
Source organism: Streptococcus pneumoniae TIGR4
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: A0A0H2URR1 (Residues: 1-172; Coverage: 100%)
Gene name: SP_1943
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand ACO 6 x ACO
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P21212
Unit cell:
a: 133.131Å b: 174.792Å c: 56.573Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.208 0.251
Expression system: Escherichia coli BL21