4hq6

X-ray diffraction
2.7Å resolution

BC domain in the presence of citrate

Released:
Source organism: Homo sapiens
Primary publication:
Structural Insights into the Regulation of ACC2 by Citrate
Bull.Korean Chem.Soc. 34 565-568 (2013)

Function and Biology Details

Reaction catalysed:
ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate + malonyl-CoA
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-126388 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetyl-CoA carboxylase 2 Chain: A
Molecule details ›
Chain: A
Length: 573 amino acids
Theoretical weight: 63.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00763 (Residues: 217-776; Coverage: 23%)
Gene names: ACACB, ACC2, ACCB
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: P3221
Unit cell:
a: 75.595Å b: 75.595Å c: 188.783Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.221 0.221 0.273
Expression system: Escherichia coli