5bqj

Structure of the yeast F1FO ATPase C10 ring with 21-hydroxy-oligomycin

Method: X-RAY DIFFRACTION Dmax: 86.8 Å Quality: GOOD

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

ATP synthase subunit 9, 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 A; UniProt 2–76 Chain B; UniProt 2–76 Chain C; UniProt 2–76 Chain D; UniProt 2–76 Chain E; UniProt 2–76 Non-standard monomer:Yes (specific site not provided by mmCIF) E21 21-hydroxy-oligomycin × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;298 K;68% MPD, 8% propylene glycol, 0.3 M sodium chloride, 2 mM magnesium sulfate, 50 mM MES, pH 5.5 Resolution 2.10 Å R-free 0.237
2 Protein homooligomer Homooligomer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain K; UniProt 2–76 Chain L; UniProt 2–76 Chain M; UniProt 2–76 Chain N; UniProt 2–76 Chain O; UniProt 2–76 Non-standard monomer:Yes (specific site not provided by mmCIF) E21 21-hydroxy-oligomycin × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;298 K;68% MPD, 8% propylene glycol, 0.3 M sodium chloride, 2 mM magnesium sulfate, 50 mM MES, pH 5.5 Resolution 2.10 Å R-free 0.237

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 52 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 A; PDBConstruct 2–76; UniProt 2–76 Author chain B; PDBConstruct 2–76; UniProt 2–76 Author chain C; PDBConstruct 2–76; UniProt 2–76 Author chain D; PDBConstruct 2–76; UniProt 2–76 Author chain E; PDBConstruct 2–76; UniProt 2–76 Author chain K; PDBConstruct 2–76; UniProt 2–76 Author chain L; PDBConstruct 2–76; UniProt 2–76 Author chain M; PDBConstruct 2–76; UniProt 2–76 Author chain N; PDBConstruct 2–76; UniProt 2–76 Author chain O; PDBConstruct 2–76; UniProt 2–76

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 5bqj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5bqj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5bqj
Deposition date deposition_date2015-05-29
Structure title titleStructure of the yeast F1FO ATPase C10 ring with 21-hydroxy-oligomycin
Keywords keywords;C10 ring, F1FO ATP synthase, 21-hydroxy-oligomycin, mitochondria, membrane, protein-antibiotic complex, MEMBRANE PROTEIN-ANTIBIOTIC complex ;; MEMBRANE PROTEIN/ANTIBIOTIC
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.44
Radius of gyration Rg (electron density) rg_electron27.32
Forward intensity I(0) i073045300.00
Molecular weight molecular_weight80905.0 kDa
Excluded volume excluded_volume107320 ų
Envelope volume envelope_volume121980 ų
Hydration-shell volume shell_volume36272 ų
Envelope diameter envelope_diameter92.7
Shell Rg shell_rg35.47
Envelope Rg envelope_rg27.37
Shape Rg shape_rg27.32
Total Rg total_rg28.28
Total atoms total_atoms5698
Residues n_residues737
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 dmax86.8
Rg (real space) rg_real28.23
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real7.3050e+07
I(0) uncertainty (real space) i0_real_error1.1320e+06
Rg (reciprocal space) rg_reciprocal28.30
I(0) (reciprocal space) i0_reciprocal73050000.0000
Solution quality estimate total_estimate0.8262
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.8
Skewness Skewness skewness0.073
Kurtosis Kurtosis kurtosis-0.438
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4101000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.916; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

Domain ID domain_id5bqjA00
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_id5bqjB00
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_id5bqjC00
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_id5bqjD00
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_id5bqjE00
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_id5bqjK00
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_id5bqjL00
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_id5bqjM00
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_id5bqjN00
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_id5bqjO00
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 (2)

9. Files and Curves (10)