PDBe 2f5z

X-ray diffraction
2.18Å resolution

Crystal Structure of Human Dihydrolipoamide Dehydrogenase (E3) Complexed to the E3-Binding Domain of Human E3-Binding Protein

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Dihydrolipoyl dehydrogenase, mitochondrial Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 474 amino acids
Theoretical weight: 50.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09622 (Residues: 36-509; Coverage: 93%)
Gene names: DLD, GCSL, LAD, PHE3
Sequence domains:
Structure domains:
Pyruvate dehydrogenase protein X component, mitochondrial Chains: K, L, M, N, O
Molecule details ›
Chains: K, L, M, N, O
Length: 64 amino acids
Theoretical weight: 7.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O00330 (Residues: 173-230; Coverage: 12%)
Gene names: PDHX, PDX1
Sequence domains: e3 binding domain
Structure domains: E3-binding domain

Ligands and Environments


Cofactor: Ligand FAD 10 x FAD
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 171.153Å b: 187.728Å c: 224.392Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.205 0.242
Expression systems:
  • Escherichia coli
  • Escherichia coli BL21