Function and Biology Details
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- NADH-quinone oxidoreductase subunit E-like
- NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain
- NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain superfamily
- NADH:ubiquinone oxidoreductase, 51kDa subunit, conserved site
- NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain superfamily
- Soluble ligand binding domain
- NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain
- NuoE domain
2 more domains
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
NADH-quinone oxidoreductase (preferred)
PDBe Complex ID:
PDB-CPX-130389 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
NADH-quinone oxidoreductase subunit E
Molecule details ›
Chains: A, C
Length: 160 amino acids
Theoretical weight: 18.57 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli
UniProt:
Sequence domains: Thioredoxin-like [2Fe-2S] ferredoxin
Length: 160 amino acids
Theoretical weight: 18.57 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli
UniProt:
- Canonical:
O66842 (Residues: 1-160; Coverage: 100%)
Sequence domains: Thioredoxin-like [2Fe-2S] ferredoxin
NADH-quinone oxidoreductase subunit F
Molecule details ›
Chains: B, D
Length: 434 amino acids
Theoretical weight: 48.52 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 434 amino acids
Theoretical weight: 48.52 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli
UniProt:
- Canonical: O66841 (Residues: 1-426; Coverage: 100%)
Sequence domains:
