3B96
Structural Basis for Substrate Fatty-Acyl Chain Specificity: Crystal Structure of Human Very-Long-Chain Acyl-CoA Dehydrogenase
Summary for 3B96
Entry DOI | 10.2210/pdb3b96/pdb |
Descriptor | Very long-chain specific acyl-CoA dehydrogenase, TETRADECANOYL-COA, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total) |
Functional Keywords | acyl-coa, fatty acid beta-oxidation, dehydrogenase, very long chain, mitochondria, membrane, acetylation, alternative splicing, cardiomyopathy, disease mutation, fad, fatty acid metabolism, flavoprotein, lipid metabolism, mitochondrion, oxidoreductase, polymorphism, transit peptide, ubl conjugation |
Biological source | Homo sapiens (human) |
Cellular location | Mitochondrion inner membrane: P49748 |
Total number of polymer chains | 1 |
Total formula weight | 65223.31 |
Authors | McAndrew, R.P.,Wang, Y.,Mohsen, A.W.,He, M.,Vockley, J.,Kim, J.J. (deposition date: 2007-11-02, release date: 2008-02-12, Last modification date: 2024-02-21) |
Primary citation | McAndrew, R.P.,Wang, Y.,Mohsen, A.W.,He, M.,Vockley, J.,Kim, J.J. Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. J.Biol.Chem., 283:9435-9443, 2008 Cited by PubMed: 18227065DOI: 10.1074/jbc.M709135200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.91 Å) |
Structure validation
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