PDBe 1fft

X-ray diffraction
3.5Å resolution

The structure of ubiquinol oxidase from Escherichia coli

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Cytochrome bo(3) ubiquinol oxidase subunit 1 Chains: A, F
Molecule details ›
Chains: A, F
Length: 663 amino acids
Theoretical weight: 74.42 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ABI8 (Residues: 1-663; Coverage: 100%)
Gene names: JW0421, b0431, cyoB
Sequence domains: Cytochrome C and Quinol oxidase polypeptide I
Structure domains: Cytochrome C Oxidase, chain A
Cytochrome bo(3) ubiquinol oxidase subunit 2 Chains: B, G
Molecule details ›
Chains: B, G
Length: 315 amino acids
Theoretical weight: 34.95 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ABJ1 (Residues: 1-315; Coverage: 100%)
Gene names: JW0422, b0432, cyoA
Sequence domains:
Structure domains:
Cytochrome bo(3) ubiquinol oxidase subunit 3 Chains: C, H
Molecule details ›
Chains: C, H
Length: 204 amino acids
Theoretical weight: 22.64 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ABJ3 (Residues: 24-204; Coverage: 89%)
Gene names: JW0420, b0430, cyoC
Structure domains: Four Helix Bundle (Hemerythrin (Met), subunit A)
UBIQUINOL OXIDASE Chains: D, I
Molecule details ›
Chains: D, I
Length: 109 amino acids
Theoretical weight: 9.29 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: C2221
Unit cell:
a: 92.1Å b: 372.5Å c: 232.7Å
α: 90° β: 90° γ: 90°
Expression system: Escherichia coli