› 2kcc

Solution NMR

Solution Structure of biotinoyl domain from human acetyl-CoA carboxylase 2

Released:
DOI: 10.2210/pdb2kcc/pdb
PDB entry 2kcc coloured by chain, ensemble of 20 models, front view.
PDB entry 2kcc coloured by chain, ensemble of 20 models, side view.
PDB entry 2kcc coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Biotinoyl domain of human acetyl-CoA carboxylase: Structural insights into the carboxyl transfer mechanism.
Lee CK, Cheong HK, Ryu KS, Lee JI, Lee W, Jeon YH, Cheong C
Proteins 72 613-24 (2008)
PMID: 18247344

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: 84 amino acids
Theoretical weight: 9.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00763 (Residues: 891-965; Coverage: 3%)
Gene names: ACACB, ACC2, ACCB
Sequence domains: Biotin-requiring enzyme
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

3 mentions without citation

Specificity and selectivity in post-translational biotin addition.
Beckett D. (2018)
2 more