› 1ebd

X-ray diffraction
2.6Å resolution

DIHYDROLIPOAMIDE DEHYDROGENASE COMPLEXED WITH THE BINDING DOMAIN OF THE DIHYDROLIPOAMIDE ACETYLASE

Released:
DOI: 10.2210/pdb1ebd/pdb
PDB entry 1ebd coloured by chain, front view.
PDB entry 1ebd coloured by chain, side view.
PDB entry 1ebd coloured by chain, top view.
Source organism: Geobacillus stearothermophilus
Primary publication:
Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase.
Mande SS, Sarfaty S, Allen MD, Perham RN, Hol WG
Structure 4 277-86 (1996)
PMID: 8805537

Function and Biology Details

Reactions catalysed: 
Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH
Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146010 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Dihydrolipoyl dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 455 amino acids
Theoretical weight: 47.8 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: P11959 (Residues: 7-461; Coverage: 97%)
Gene name: pdhD
Sequence domains:
Structure domains:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex Chain: C
Molecule details ›
Chain: C
Length: 41 amino acids
Theoretical weight: 4.44 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: P11961 (Residues: 130-170; Coverage: 10%)
Gene name: pdhC
Sequence domains: e3 binding domain
Structure domains: E3-binding domain

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 106.6Å b: 106.6Å c: 204.3Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.215 not available
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions.
Perham RN. (2000)
7 more

20 mentions without citation

What lessons can be learned from studying the folding of homologous proteins?
Nickson et al. (2010)
19 more