› 1aqt

X-ray diffraction
2.3Å resolution

EPSILON SUBUNIT OF F1F0-ATP SYNTHASE FROM ESCHERICHIA COLI

Released:
DOI: 10.2210/pdb1aqt/pdb
PDB entry 1aqt coloured by chain, front view.
PDB entry 1aqt coloured by chain, side view.
PDB entry 1aqt coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli.
Uhlin U, Cox GB, Guss JM
Structure 5 1219-30 (1997)
PMID: 9331422

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141307 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP synthase epsilon chain Chain: A
Molecule details ›
Chain: A
Length: 138 amino acids
Theoretical weight: 14.9 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6E6 (Residues: 4-139; Coverage: 98%)
Gene names: JW3709, atpC, b3731, papG, uncC
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P6522
Unit cell:
a: 94.61Å b: 94.61Å c: 56.92Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.214 0.214 0.288
Expression system: Escherichia coli

Quick links

Citations

17 review citations

ATP synthase--a marvellous rotary engine of the cell.
Yoshida et al. (2001)
16 more

18 mentions without citation

Insights into the regulatory function of the ɛ subunit from bacterial F-type ATP synthases: a comparison of structural, biochemical and biophysical data.
Krah et al. (2018)
17 more