› 1egc

X-ray diffraction
2.6Å resolution

STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA DEHYDROGENASE COMPLEXED WITH OCTANOYL-COA

Released:
DOI: 10.2210/pdb1egc/pdb
PDB entry 1egc coloured by chain, front view.
PDB entry 1egc coloured by chain, side view.
PDB entry 1egc coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity.
Lee HJ, Wang M, Paschke R, Nandy A, Ghisla S, Kim JJ
Biochemistry 35 12412-20 (1996)
PMID: 8823176

Function and Biology Details

Reaction catalysed: 
A medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145791 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Medium-chain specific acyl-CoA dehydrogenase, mitochondrial Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 396 amino acids
Theoretical weight: 43.65 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P11310 (Residues: 26-421; Coverage: 94%)
Gene name: ACADM
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 4 x FAD
1 bound ligand:
Ligand CO8 4 x CO8
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43212
Unit cell:
a: 170Å b: 170Å c: 149.87Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.217 not available
Expression system: Not provided

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Citations

6 review citations

Mutation analysis in mitochondrial fatty acid oxidation defects: Exemplified by acyl-CoA dehydrogenase deficiencies, with special focus on genotype-phenotype relationship.
Gregersen et al. (2001)
5 more

4 mentions without citation

Mycobacterium tuberculosis utilizes a unique heterotetrameric structure for dehydrogenation of the cholesterol side chain.
Thomas et al. (2013)
3 more