PDBe 6dv2

X-ray diffraction
3.6Å resolution

Crystal Structure of Human Mitochondrial Trifunctional Protein

Released:
Source organism: Homo sapiens
Entry authors: Fu Z, Xia C, Battaile KP, Kim JP

Function and Biology Details

Reactions catalysed:
Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
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
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 beta, mitochondrial Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 457 amino acids
Theoretical weight: 49.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P55084 (Residues: 34-474; Coverage: 93%)
Gene names: HADHB, MSTP029
Sequence domains:
Trifunctional enzyme subunit alpha, mitochondrial Chains: G, H, I, J, K, L
Molecule details ›
Chains: G, H, I, J, K, L
Length: 727 amino acids
Theoretical weight: 79.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P40939 (Residues: 37-763; Coverage: 95%)
Gene names: HADH, HADHA
Sequence domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-BM
Spacegroup: P21
Unit cell:
a: 136.536Å b: 237.938Å c: 141.319Å
α: 90° β: 105.61° γ: 90°
R-values:
R R work R free
0.244 0.244 0.289
Expression system: Escherichia coli BL21(DE3)