3u2y

ATP synthase c10 ring in proton-unlocked conformation at pH 6.1

Method: X-RAY DIFFRACTION Dmax: 77.3 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

ATP synthase subunit C, mitochondrial

OrganismNot specified

UniProt P61829

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain K; UniProt 1–76 Chain L; UniProt 1–76 Chain M; UniProt 1–76 Chain N; UniProt 1–76 Chain O; UniProt 1–76 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.1;294 K;68% MPD, 8% propolyene glycol, 0.3M NaCl, 0.1M malonate pH 7.0, 2mM MgSO4, 50 mM MES pH 6.1, VAPOR DIFFUSION, SITTING DROP, temperature 294K Resolution 2.50 Å R-free 0.227

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

48 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP9_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain K; PDBConstruct 1–76; UniProt 1–76 Author chain L; PDBConstruct 1–76; UniProt 1–76 Author chain M; PDBConstruct 1–76; UniProt 1–76 Author chain N; PDBConstruct 1–76; UniProt 1–76 Author chain O; PDBConstruct 1–76; UniProt 1–76

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 3u2y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3u2y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3u2y
Deposition date deposition_date2011-10-04
Structure title titleATP synthase c10 ring in proton-unlocked conformation at pH 6.1
Keywords keywordsF1FO ATP synthase, proton pore, c10 ring, membrane protein; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier22.74
Radius of gyration Rg (electron density) rg_electron22.15
Forward intensity I(0) i018357800.00
Molecular weight molecular_weight37714.0 kDa
Excluded volume excluded_volume49499 ų
Envelope volume envelope_volume55494 ų
Hydration-shell volume shell_volume21206 ų
Envelope diameter envelope_diameter76.7
Shell Rg shell_rg28.70
Envelope Rg envelope_rg22.67
Shape Rg shape_rg22.15
Total Rg total_rg23.14
Total atoms total_atoms2655
Residues n_residues368
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax77.3
Rg (real space) rg_real22.79
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real1.8360e+07
I(0) uncertainty (real space) i0_real_error2.1680e+05
Rg (reciprocal space) rg_reciprocal22.78
I(0) (reciprocal space) i0_reciprocal18360000.0000
Solution quality estimate total_estimate0.8861
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.9
Skewness Skewness skewness0.367
Kurtosis Kurtosis kurtosis-0.368
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2843000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.867; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.925; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 5 domains

CATH v4.4 (5 domains)

Domain ID domain_id3u2yK00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id3u2yL00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id3u2yM00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id3u2yN00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id3u2yO00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C

8. Citations (1)

9. Files and Curves (10)