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X-ray diffraction
3.01Å resolution

Refined structure of yeast F1c10 ATPase complex to 3 A resolution

Released:
Source organism: Saccharomyces cerevisiae
Primary publication:
Molecular architecture of the rotary motor in ATP synthase.
Science 286 1700-5 (1999)
PMID: 10576729

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero nonadecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123198 (preferred)
Entry contents:
6 distinct polypeptide molecules
Macromolecules (6 distinct):
ATP synthase subunit alpha, mitochondrial Chains: A, B, C
ATP synthase subunit beta, mitochondrial Chains: D, E, F
ATP synthase subunit gamma, mitochondrial Chain: G
Molecule details ›
Chain: G
Length: 311 amino acids
Theoretical weight: 34.4 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
  • Canonical: P38077 (Residues: 1-311; Coverage: 100%)
Gene names: ATP3, ATP3a, ATP3b, YBR039W, YBR0408
Sequence domains: ATP synthase
Structure domains:
ATP synthase subunit delta, mitochondrial Chain: H
Molecule details ›
Chain: H
Length: 160 amino acids
Theoretical weight: 17.04 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
  • Canonical: Q12165 (Residues: 1-160; Coverage: 100%)
Gene names: ATP16, D2935, YD8119.03, YDL004W
Sequence domains:
Structure domains: F0F1 ATP synthase delta/epsilon subunit, N-terminal
ATP synthase catalytic sector F1 epsilon subunit Chain: I
Molecule details ›
Chain: I
Length: 61 amino acids
Theoretical weight: 6.64 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
  • Canonical: E9P9X4 (Residues: 2-62; Coverage: 98%)
Sequence domains: Mitochondrial ATP synthase epsilon chain
Structure domains: ATP synthase, F1 complex, epsilon subunit superfamily, mitochondrial
ATP synthase subunit 9, mitochondrial Chains: K, L, M, N, O, P, Q, R, S, T
Molecule details ›
Chains: K, L, M, N, O, P, Q, R, S, T
Length: 76 amino acids
Theoretical weight: 7.76 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
  • Canonical: P61829 (Residues: 1-76; Coverage: 100%)
Gene names: ATP9, OLI1, OLI3, PHO2, Q0130
Sequence domains: ATP synthase subunit C
Structure domains: F1F0 ATP synthase subunit C

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 135.352Å b: 173.711Å c: 137.889Å
α: 90° β: 91.77° γ: 90°
R-values:
R R work R free
0.211 0.21 0.253