6q9g

X-ray diffraction
2.1Å resolution

Crystal structure of reduced Aquifex aeolicus NADH-quinone oxidoreductase subunits NuoE G129D and NuoF bound to NADH

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-130389 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
NADH-quinone oxidoreductase subunit E Chains: A, C
Molecule details ›
Chains: A, C
Length: 160 amino acids
Theoretical weight: 18.63 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O66842 (Residues: 1-160; Coverage: 100%)
Gene names: aq_574, nuoE
Sequence domains: Thioredoxin-like [2Fe-2S] ferredoxin
NADH-quinone oxidoreductase subunit F Chains: B, D
Molecule details ›
Chains: B, D
Length: 434 amino acids
Theoretical weight: 48.52 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O66841 (Residues: 1-426; Coverage: 100%)
Gene names: aq_573, nuoF
Sequence domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 63.33Å b: 116.18Å c: 189.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.191 0.231
Expression system: Escherichia coli BL21(DE3)