PDBe 5zqz

Electron Microscopy
4.2Å resolution

Structure of human mitochondrial trifunctional protein, tetramer

Released:
Source organism: Homo sapiens
Primary publication:
Cryo-EM structure of human mitochondrial trifunctional protein.
Proc. Natl. Acad. Sci. U.S.A. (2018)
PMID: 29915090
Related structures: EMD-6940

Function and Biology Details

Reactions catalysed:
A long-chain (S)-3-hydroxyacyl-CoA + NAD(+) = a long-chain 3-oxoacyl-CoA + NADH
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O
Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Trifunctional enzyme subunit alpha, mitochondrial Chains: A, C
Molecule details ›
Chains: A, C
Length: 763 amino acids
Theoretical weight: 83.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P40939 (Residues: 1-763; Coverage: 100%)
Gene names: HADH, HADHA
Sequence domains:
Trifunctional enzyme subunit beta, mitochondrial Chains: B, D
Molecule details ›
Chains: B, D
Length: 474 amino acids
Theoretical weight: 51.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55084 (Residues: 1-474; Coverage: 100%)
Gene names: HADHB, MSTP029
Sequence domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 4.2Å
Relevant EMDB volumes: EMD-6940
Expression system: Escherichia coli