› 3glk

X-ray diffraction
2.1Å resolution

The biotin carboxylase (BC) domain of human Acetyl-CoA Carboxylase 2 (ACC2)

Released:
DOI: 10.2210/pdb3glk/pdb
PDB entry 3glk coloured by chain, front view.
PDB entry 3glk coloured by chain, side view.
PDB entry 3glk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Synthesis and characterization of a BODIPY-labeled derivative of Soraphen A that binds to acetyl-CoA carboxylase.
Raymer B, Kavana M, Price A, Wang B, Corcoran L, Kulathila R, Groarke J, Mann T
Bioorg Med Chem Lett 19 2804-7 (2009)
PMID: 19359168

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
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: 540 amino acids
Theoretical weight: 60.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00763 (Residues: 238-760; Coverage: 21%)
Gene names: ACACB, ACC2, ACCB
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P4322
Unit cell:
a: 97.536Å b: 97.536Å c: 127.157Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.212 0.247
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Structure and function of biotin-dependent carboxylases.
Tong L. (2013)
7 other articles

5 mentions without citation

Acetyl-CoA carboxylase inhibition by ND-630 reduces hepatic steatosis, improves insulin sensitivity, and modulates dyslipidemia in rats.
Harriman et al. (2016)
4 more