4f4s

Structure of the yeast F1Fo ATPase c10 ring with bound oligomycin

Method: X-RAY DIFFRACTION Dmax: 89.5 Å Quality: GOOD

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

ATP synthase subunit 9, mitochondrial

Saccharomyces cerevisiae

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 1–76 Chain B; UniProt 1–76 Chain C; UniProt 1–76 Chain D; UniProt 1–76 Chain E; UniProt 1–76 Non-standard monomer:Yes (specific site not provided by mmCIF) EFO Oligomycin A × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;298 K;68% MPD, 8% PROPYLENE GLYCOL, 0.3M NACL, 2MM MGSO4, 50MM MES PH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 1.90 Å R-free 0.228
2 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) EFO Oligomycin A × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;298 K;68% MPD, 8% PROPYLENE GLYCOL, 0.3M NACL, 2MM MGSO4, 50MM MES PH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 1.90 Å R-free 0.228

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 1–76; UniProt 1–76 Author chain B; PDBConstruct 1–76; UniProt 1–76 Author chain C; PDBConstruct 1–76; UniProt 1–76 Author chain D; PDBConstruct 1–76; UniProt 1–76 Author chain E; PDBConstruct 1–76; UniProt 1–76 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 4f4s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4f4s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4f4s
Deposition date deposition_date2012-05-11
Structure title titleStructure of the yeast F1Fo ATPase c10 ring with bound oligomycin
Keywords keywordsc10 ring, F1Fo ATP synthase, Oligomycin, mitochondria, 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_guinier28.41
Radius of gyration Rg (electron density) rg_electron27.27
Forward intensity I(0) i073020200.00
Molecular weight molecular_weight80819.0 kDa
Excluded volume excluded_volume107220 ų
Envelope volume envelope_volume121950 ų
Hydration-shell volume shell_volume36329 ų
Envelope diameter envelope_diameter92.6
Shell Rg shell_rg35.36
Envelope Rg envelope_rg27.31
Shape Rg shape_rg27.27
Total Rg total_rg28.25
Total atoms total_atoms5693
Residues n_residues739
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 dmax89.5
Rg (real space) rg_real28.20
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real7.3020e+07
I(0) uncertainty (real space) i0_real_error1.0040e+06
Rg (reciprocal space) rg_reciprocal28.26
I(0) (reciprocal space) i0_reciprocal73020000.0000
Solution quality estimate total_estimate0.8924
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.4
Skewness Skewness skewness0.072
Kurtosis Kurtosis kurtosis-0.436
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4171000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.887; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.944

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_id4f4sA00
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_id4f4sB00
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_id4f4sC00
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_id4f4sD00
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_id4f4sE00
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_id4f4sK00
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_id4f4sL00
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_id4f4sM00
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_id4f4sN00
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_id4f4sO00
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)