4g73

X-ray diffraction
2.52Å resolution

Crystal structure of NDH with NADH and Quinone

Released:

Function and Biology Details

Reaction catalysed:
NADH + a quinone = NAD(+) + a quinol
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-152272 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rotenone-insensitive NADH-ubiquinone oxidoreductase, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 502 amino acids
Theoretical weight: 56.07 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P32340 (Residues: 24-513; Coverage: 96%)
Gene names: NDI1, YM7056.06C, YML120C
Sequence domains: Pyridine nucleotide-disulphide oxidoreductase
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments


Cofactor: Ligand NAI 2 x NAI

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: C2221
Unit cell:
a: 127.406Å b: 230.186Å c: 112.921Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.189 0.218
Expression system: Escherichia coli