6bn2

X-ray diffraction
1.65Å resolution

Crystal structure of Acetyl-CoA acetyltransferase from Elizabethkingia anophelis NUHP1

Released:
Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Reaction catalysed:
(1a) acetyl-CoA + [acetyl-CoA C-acetyltransferase]-L-cysteine = [acetyl-CoA C-acetyltransferase]-S-acetyl-L-cysteine + CoA
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:
Acetyl-CoA acetyltransferase Chain: A
Molecule details ›
Chain: A
Length: 401 amino acids
Theoretical weight: 42.35 KDa
Source organism: Elizabethkingia anophelis NUHP1
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: A0A077EEP0 (Residues: 1-392; Coverage: 100%)
Gene name: BD94_2261
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: C222
Unit cell:
a: 99.17Å b: 167.42Å c: 72.56Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.139 0.138 0.156
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'