› 3tdc

X-ray diffraction
2.41Å resolution

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

Assemblies composition:
monomeric (preferred)
homo dimer
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: 762 amino acids
Theoretical weight: 86.59 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: O00763 (Residues: 1690-2445; Coverage: 31%)
Gene names: ACACB, ACC2, ACCB
Sequence domains: Carboxyl transferase domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 0EU 1 x 0EU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: C2221
Unit cell:
a: 113.921Å b: 119.756Å c: 146.035Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.169 0.218
Expression system: Spodoptera frugiperda

Quick links

Citations

2 review citations

Structure and function of biotin-dependent carboxylases.
Tong L. (2013)
1 more

1 mention without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)