2cly

X-ray diffraction
2.8Å resolution

Subcomplex of the stator of bovine mitochondrial ATP synthase

Released:
Source organism: Bos taurus

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
ATP synthase F(0) complex subunit B1, mitochondrial Chains: A, D
Molecule details ›
Chains: A, D
Length: 214 amino acids
Theoretical weight: 24.7 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P13619 (Residues: 43-256; Coverage: 84%)
Gene names: ATP5F, ATP5F1, ATP5PB
Sequence domains: Mitochondrial ATP synthase B chain precursor (ATP-synt_B)
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
ATP synthase subunit d, mitochondrial Chains: B, E
Molecule details ›
Chains: B, E
Length: 160 amino acids
Theoretical weight: 18.59 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P13620 (Residues: 2-161; Coverage: 99%)
Gene names: ATP5H, ATP5PD
Sequence domains: ATP synthase D chain, mitochondrial (ATP5H)
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1
ATP synthase-coupling factor 6, mitochondrial Chains: C, F
Molecule details ›
Chains: C, F
Length: 77 amino acids
Theoretical weight: 9.12 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P02721 (Residues: 32-108; Coverage: 71%)
Gene names: ATP5J, ATP5PF
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 50.499Å b: 79.354Å c: 115.665Å
α: 90° β: 93.08° γ: 90°
R-values:
R R work R free
0.234 0.231 0.295
Expression system: Escherichia coli BL21(DE3)