PDBe 1zy8

X-ray diffraction
2.59Å resolution

The crystal structure of dihydrolipoamide dehydrogenase and dihydrolipoamide dehydrogenase-binding protein (didomain) subcomplex of human pyruvate dehydrogenase complex.

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: 50.24 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, OA
Molecule details ›
Chains: K, L, M, N, OA
Length: 229 amino acids
Theoretical weight: 24.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O00330 (Residues: 54-274; Coverage: 44%)
  • Best match: O00330-2 (Residues: 54-114)
Gene names: PDHX, PDX1
Sequence domains:
Structure domains: E3-binding domain

Ligands and Environments


Cofactor: Ligand FAD 10 x FAD
No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 168.79Å b: 186.91Å c: 217.54Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.275 0.208 0.276
Expression systems:
  • Escherichia coli
  • Escherichia coli BL21