2w6i

X-ray diffraction
4Å resolution

Low resolution structures of bovine mitochondrial F1-ATPase during controlled dehydration: Hydration State 4B.

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero nonamer (preferred)
PDBe Complex ID:
PDB-CPX-133621 (preferred)
Entry contents:
5 distinct polypeptide molecules
Macromolecules (5 distinct):
ATP synthase subunit alpha, mitochondrial Chains: A, B, C
ATP synthase subunit beta, mitochondrial Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 528 amino acids
Theoretical weight: 56.34 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00829 (Residues: 1-528; Coverage: 100%)
Gene names: ATP5B, ATP5F1B
Sequence domains:
Structure domains:
ATP synthase subunit gamma, mitochondrial Chain: G
Molecule details ›
Chain: G
Length: 298 amino acids
Theoretical weight: 33.12 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P05631 (Residues: 1-298; Coverage: 100%)
Gene names: ATP5C, ATP5C1, ATP5F1C
Sequence domains: ATP synthase
Structure domains:
ATP synthase subunit delta, mitochondrial Chain: H
Molecule details ›
Chain: H
Length: 168 amino acids
Theoretical weight: 17.63 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P05630 (Residues: 1-168; Coverage: 100%)
Gene names: ATP5D, ATP5F1D
Sequence domains:
ATP synthase subunit epsilon, mitochondrial Chain: I
Molecule details ›
Chain: I
Length: 51 amino acids
Theoretical weight: 5.79 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P05632 (Residues: 1-51; Coverage: 100%)
Gene names: ATP5E, ATP5F1E
Sequence domains: Mitochondrial ATP synthase epsilon chain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 108.92Å b: 131.33Å c: 267.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.299 0.299 0.3