2jj2

X-ray diffraction
2.4Å resolution

The Structure of F1-ATPase inhibited by quercetin.

Released:
Source organism: Bos taurus
Primary publication:
Mechanism of inhibition of bovine F1-ATPase by resveratrol and related polyphenols.
Proc. Natl. Acad. Sci. U.S.A. 104 13632-7 (2007)
PMID: 17698806

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero heptamer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
ATP synthase subunit alpha, mitochondrial Chains: A, B, C, H, I, J
Molecule details ›
Chains: A, B, C, H, I, J
Length: 510 amino acids
Theoretical weight: 55.33 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P19483 (Residues: 44-553; Coverage: 92%)
Gene names: ATP5A1, ATP5A2, ATP5F1A
Sequence domains:
Structure domains:
ATP synthase subunit beta, mitochondrial Chains: D, E, F, K, L, M
Molecule details ›
Chains: D, E, F, K, L, M
Length: 482 amino acids
Theoretical weight: 51.76 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00829 (Residues: 47-528; Coverage: 91%)
Gene names: ATP5B, ATP5F1B
Sequence domains:
Structure domains:
ATP synthase subunit gamma, mitochondrial Chains: G, N
Molecule details ›
Chains: G, N
Length: 272 amino acids
Theoretical weight: 30.19 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P05631 (Residues: 26-297; Coverage: 91%)
Gene names: ATP5C, ATP5C1, ATP5F1C
Sequence domains: ATP synthase
Structure domains:

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 106.399Å b: 282.019Å c: 138.093Å
α: 90° β: 90.44° γ: 90°
R-values:
R R work R free
0.19 0.188 0.238