› 3urh

X-ray diffraction
1.9Å resolution

Crystal structure of a dihydrolipoamide dehydrogenase from Sinorhizobium meliloti 1021

Released:
DOI: 10.2210/pdb3urh/pdb
PDB entry 3urh coloured by chain, front view.
PDB entry 3urh coloured by chain, side view.
PDB entry 3urh coloured by chain, top view.
Source organism: Sinorhizobium meliloti 1021
Entry authors: Kumaran D, Chamala S, Evans B, Foti R, Gizzi A, Hillerich B, Kar A, LaFleur J, Seidel R, Villigas G, Zencheck W, Almo SC, Swaminathan S, New York Structural Genomics Research Consortium (NYSGRC)

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-187877 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrolipoyl dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 491 amino acids
Theoretical weight: 52.26 KDa
Source organism: Sinorhizobium meliloti 1021
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92LK0 (Residues: 1-468; Coverage: 100%)
Gene names: SMc02487, lpdA2
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
2 bound ligands:
Ligand SO4 2 x SO4
Ligand EDO 1 x EDO
1 modified residue:
Ligand MSE 32 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 74.433Å b: 104.716Å c: 120.622Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.184 0.227
Expression system: Escherichia coli

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