› 4jdr

X-ray diffraction
2.5Å resolution

Function and Biology Details

Reaction catalysed: 
Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141908 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrolipoyl dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 474 amino acids
Theoretical weight: 50.76 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A9P0 (Residues: 1-474; Coverage: 100%)
Gene names: JW0112, b0116, lpd, lpdA
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
2 bound ligands:
Ligand MES 3 x MES
Ligand SO4 7 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: I422
Unit cell:
a: 180Å b: 180Å c: 196.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.214 0.256
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Applications of hydrogen/deuterium exchange MS from 2012 to 2014.
Pirrone et al. (2015)
4 more

6 mentions without citation

The pyruvate dehydrogenase complexes: structure-based function and regulation.
Patel et al. (2014)
5 more