› 4f0x

X-ray diffraction
3.29Å resolution

Crystal structure of human Malonyl-CoA Decarboxylase (Peroxisomal Isoform)

Released:
DOI: 10.2210/pdb4f0x/pdb
PDB entry 4f0x coloured by chain, front view.
PDB entry 4f0x coloured by chain, side view.
PDB entry 4f0x coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural asymmetry and disulfide bridges among subunits modulate the activity of human malonyl-CoA decarboxylase.
Aparicio D, Pérez-Luque R, Carpena X, Díaz M, Ferrer JC, Loewen PC, Fita I
J Biol Chem 288 11907-19 (2013)
PMID: 23482565

Function and Biology Details

Reaction catalysed: 
Malonyl-CoA = acetyl-CoA + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132058 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Malonyl-CoA decarboxylase, mitochondrial Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 458 amino acids
Theoretical weight: 51.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O95822 (Residues: 39-493; Coverage: 92%)
Gene name: MLYCD
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 0OR 4 x 0OR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P1
Unit cell:
a: 80.42Å b: 103.31Å c: 134.24Å
α: 95.32° β: 90.22° γ: 94.46°
R-values:
R R work R free
0.246 0.244 0.267
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 citation in other articles

Malonyl CoA Decarboxylase Inhibition Improves Cardiac Function Post-Myocardial Infarction.
Wang et al. (2019)
7 more

1 mention without citation

Structural asymmetry and disulfide bridges among subunits modulate the activity of human malonyl-CoA decarboxylase.
Aparicio et al. (2013)