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: 18227065 DOI: 10.1074/jbc.M709135200 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.91 Å)

Structure validation