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2KCC

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

Summary for 2KCC
Entry DOI10.2210/pdb2kcc/pdb
DescriptorAcetyl-CoA carboxylase 2 (1 entity in total)
Functional Keywordsacetyl-coa carboxylase, biotinoyl domain, bccp, bira, biotinylation, alternative splicing, atp-binding, biotin, fatty acid biosynthesis, ligase, lipid synthesis, manganese, membrane, metal-binding, multifunctional enzyme, nucleotide-binding, phosphoprotein, polymorphism
Biological sourceHomo sapiens (Human)
Cellular locationEndomembrane system: O00763
Total number of polymer chains1
Total formula weight9423.71
Authors
Lee, C.,Cheong, H.,Ryu, K.,Lee, J.,Lee, W.,Jeon, Y.,Cheong, C. (deposition date: 2008-12-19, release date: 2009-02-17, Last modification date: 2023-09-27)
Primary citationLee, C.K.,Cheong, H.K.,Ryu, K.S.,Lee, J.I.,Lee, W.,Jeon, Y.H.,Cheong, C.
Biotinoyl domain of human acetyl-CoA carboxylase: Structural insights into the carboxyl transfer mechanism.
Proteins, 72:613-624, 2008
Cited by
PubMed: 18247344
DOI: 10.1002/prot.21952
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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