3GID

The biotin carboxylase (BC) domain of human Acetyl-CoA Carboxylase 2 (ACC2) in complex with Soraphen A

Summary for 3GID

• Entry DOI: 10.2210/pdb3gid/pdb
• Descriptor: Acetyl-CoA carboxylase 2, SORAPHEN A (3 entities in total)
• Functional Keywords: atp binding, carboxylase, atp-binding, biotin, fatty acid biosynthesis, ligase, lipid synthesis, manganese, membrane, metal-binding, multifunctional enzyme, nucleotide-binding, phosphoprotein
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion : O00763
• Total number of polymer chains: 2
• Total formula weight: 121227.21

Authors

Price, A.,Kulathila, R. (deposition date: 2009-03-05, release date: 2009-03-17, Last modification date: 2024-02-21)

Primary citation

Raymer, B.,Kavana, M.,Price, A.,Wang, B.,Corcoran, L.,Kulathila, R.,Groarke, J.,Mann, T.
Synthesis and characterization of a BODIPY-labeled derivative of Soraphen A that binds to acetyl-CoA carboxylase.
Bioorg.Med.Chem.Lett., 19:2804-2807, 2009

PubMed Abstract: BODIPY-labeled Soraphen A derivative 4 was synthesized and characterized as an acetyl-CoA carboxylase (ACC) binder. Biophysical measurements indicate that the molecule binds in the biotin carboxylase domain where Soraphen A has been shown to bind. The fluorescent label of the BODIPY can be used to biophysically identify a compound that binds to the Soraphen A site of the biotin carboxylase domain versus the carboxytransferase domain of ACC.

PubMed: 19359168
DOI: 10.1016/j.bmcl.2009.03.107

Experimental method

X-RAY DIFFRACTION (2.3 Å)