6yy0

bovine ATP synthase F1-peripheral stalk domain, state 1

Method: ELECTRON MICROSCOPY Dmax: 166.4 Å Quality: GOOD

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

ATP synthase subunit alpha, mitochondrial

OrganismNot specified

UniProt P19483

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 heterocomplex Heteromer Protein × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain A; UniProt 44–553 Chain B; UniProt 44–553 Chain C; UniProt 44–553 Not recorded ATP synthase subunit beta, mitochondrial × 3 (P00829) ATP synthase subunit gamma, mitochondrial × 1 (P05631) ATP synthase subunit delta, mitochondrial × 1 (P05630) ATP synthase subunit epsilon, mitochondrial × 1 (P05632) ATPase inhibitor, mitochondrial × 1 (P01096) ATP synthase subunit O, mitochondrial × 1 (P13621) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) ATP synthase subunit d, mitochondrial × 1 (P13620) ATP synthase-coupling factor 6, mitochondrial × 1 (P02721) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;The sample was allowed to penetrate through the holey support and to distribute to both sides of the grid surface for ca. 15 sec. Then the grids were blotted with filter paper for 8-10 sec before blotting. Resolution 3.23 Å

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.

58 other PDB entries and 62 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPA_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–510; UniProt 44–553 Author chain B; PDBConstruct 1–510; UniProt 44–553 Author chain C; PDBConstruct 1–510; UniProt 44–553

ATP synthase subunit beta, mitochondrial

OrganismNot specified

UniProt P00829

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 heterocomplex Heteromer Protein × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain D; UniProt 47–528 Chain E; UniProt 47–528 Chain F; UniProt 47–528 Not recorded ATP synthase subunit alpha, mitochondrial × 3 (P19483) ATP synthase subunit gamma, mitochondrial × 1 (P05631) ATP synthase subunit delta, mitochondrial × 1 (P05630) ATP synthase subunit epsilon, mitochondrial × 1 (P05632) ATPase inhibitor, mitochondrial × 1 (P01096) ATP synthase subunit O, mitochondrial × 1 (P13621) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) ATP synthase subunit d, mitochondrial × 1 (P13620) ATP synthase-coupling factor 6, mitochondrial × 1 (P02721) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;The sample was allowed to penetrate through the holey support and to distribute to both sides of the grid surface for ca. 15 sec. Then the grids were blotted with filter paper for 8-10 sec before blotting. Resolution 3.23 Å

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.

55 other PDB entries and 59 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPB_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–482; UniProt 47–528 Author chain E; PDBConstruct 1–482; UniProt 47–528 Author chain F; PDBConstruct 1–482; UniProt 47–528

ATP synthase subunit gamma, mitochondrial

OrganismNot specified

UniProt P05631

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 heterocomplex Heteromer Protein × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain G; UniProt 26–298 Not recorded ATP synthase subunit alpha, mitochondrial × 3 (P19483) ATP synthase subunit beta, mitochondrial × 3 (P00829) ATP synthase subunit delta, mitochondrial × 1 (P05630) ATP synthase subunit epsilon, mitochondrial × 1 (P05632) ATPase inhibitor, mitochondrial × 1 (P01096) ATP synthase subunit O, mitochondrial × 1 (P13621) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) ATP synthase subunit d, mitochondrial × 1 (P13620) ATP synthase-coupling factor 6, mitochondrial × 1 (P02721) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;The sample was allowed to penetrate through the holey support and to distribute to both sides of the grid surface for ca. 15 sec. Then the grids were blotted with filter paper for 8-10 sec before blotting. Resolution 3.23 Å

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.

58 other PDB entries and 62 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPG_BOVIN
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–273; UniProt 26–298

ATP synthase subunit delta, mitochondrial

OrganismNot specified

UniProt P05630

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 heterocomplex Heteromer Protein × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain H; UniProt 23–168 Not recorded ATP synthase subunit alpha, mitochondrial × 3 (P19483) ATP synthase subunit beta, mitochondrial × 3 (P00829) ATP synthase subunit gamma, mitochondrial × 1 (P05631) ATP synthase subunit epsilon, mitochondrial × 1 (P05632) ATPase inhibitor, mitochondrial × 1 (P01096) ATP synthase subunit O, mitochondrial × 1 (P13621) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) ATP synthase subunit d, mitochondrial × 1 (P13620) ATP synthase-coupling factor 6, mitochondrial × 1 (P02721) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;The sample was allowed to penetrate through the holey support and to distribute to both sides of the grid surface for ca. 15 sec. Then the grids were blotted with filter paper for 8-10 sec before blotting. Resolution 3.23 Å

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.

38 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPD_BOVIN
Isoform
PDB entities 4
Chains and sequence ranges Author chain H; PDBConstruct 1–146; UniProt 23–168

ATP synthase subunit epsilon, mitochondrial

OrganismNot specified

UniProt P05632

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 heterocomplex Heteromer Protein × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain I; UniProt 2–51 Not recorded ATP synthase subunit alpha, mitochondrial × 3 (P19483) ATP synthase subunit beta, mitochondrial × 3 (P00829) ATP synthase subunit gamma, mitochondrial × 1 (P05631) ATP synthase subunit delta, mitochondrial × 1 (P05630) ATPase inhibitor, mitochondrial × 1 (P01096) ATP synthase subunit O, mitochondrial × 1 (P13621) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) ATP synthase subunit d, mitochondrial × 1 (P13620) ATP synthase-coupling factor 6, mitochondrial × 1 (P02721) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;The sample was allowed to penetrate through the holey support and to distribute to both sides of the grid surface for ca. 15 sec. Then the grids were blotted with filter paper for 8-10 sec before blotting. Resolution 3.23 Å

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.

38 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP5E_BOVIN
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 1–50; UniProt 2–51

ATPase inhibitor, mitochondrial

Bos taurus

UniProt P01096

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 heterocomplex Heteromer Protein × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain J; UniProt 26–85 Not recorded ATP synthase subunit alpha, mitochondrial × 3 (P19483) ATP synthase subunit beta, mitochondrial × 3 (P00829) ATP synthase subunit gamma, mitochondrial × 1 (P05631) ATP synthase subunit delta, mitochondrial × 1 (P05630) ATP synthase subunit epsilon, mitochondrial × 1 (P05632) ATP synthase subunit O, mitochondrial × 1 (P13621) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) ATP synthase subunit d, mitochondrial × 1 (P13620) ATP synthase-coupling factor 6, mitochondrial × 1 (P02721) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;The sample was allowed to penetrate through the holey support and to distribute to both sides of the grid surface for ca. 15 sec. Then the grids were blotted with filter paper for 8-10 sec before blotting. Resolution 3.23 Å

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.

23 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATIF1_BOVIN
Isoform
PDB entities 6
Chains and sequence ranges Author chain J; PDBConstruct 1–60; UniProt 26–85

ATP synthase subunit O, mitochondrial

OrganismNot specified

UniProt P13621

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 heterocomplex Heteromer Protein × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain S; UniProt 24–213 Not recorded ATP synthase subunit alpha, mitochondrial × 3 (P19483) ATP synthase subunit beta, mitochondrial × 3 (P00829) ATP synthase subunit gamma, mitochondrial × 1 (P05631) ATP synthase subunit delta, mitochondrial × 1 (P05630) ATP synthase subunit epsilon, mitochondrial × 1 (P05632) ATPase inhibitor, mitochondrial × 1 (P01096) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) ATP synthase subunit d, mitochondrial × 1 (P13620) ATP synthase-coupling factor 6, mitochondrial × 1 (P02721) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;The sample was allowed to penetrate through the holey support and to distribute to both sides of the grid surface for ca. 15 sec. Then the grids were blotted with filter paper for 8-10 sec before blotting. Resolution 3.23 Å

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.

30 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPO_BOVIN
Isoform
PDB entities 7
Chains and sequence ranges Author chain S; PDBConstruct 1–190; UniProt 24–213

ATP synthase F(0) complex subunit B1, mitochondrial

OrganismNot specified

UniProt P13619

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 heterocomplex Heteromer Protein × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain b; UniProt 43–256 Not recorded ATP synthase subunit alpha, mitochondrial × 3 (P19483) ATP synthase subunit beta, mitochondrial × 3 (P00829) ATP synthase subunit gamma, mitochondrial × 1 (P05631) ATP synthase subunit delta, mitochondrial × 1 (P05630) ATP synthase subunit epsilon, mitochondrial × 1 (P05632) ATPase inhibitor, mitochondrial × 1 (P01096) ATP synthase subunit O, mitochondrial × 1 (P13621) ATP synthase subunit d, mitochondrial × 1 (P13620) ATP synthase-coupling factor 6, mitochondrial × 1 (P02721) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;The sample was allowed to penetrate through the holey support and to distribute to both sides of the grid surface for ca. 15 sec. Then the grids were blotted with filter paper for 8-10 sec before blotting. Resolution 3.23 Å

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.

31 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AT5F1_BOVIN
Isoform
PDB entities 8
Chains and sequence ranges Author chain b; PDBConstruct 1–214; UniProt 43–256

ATP synthase subunit d, mitochondrial

OrganismNot specified

UniProt P13620

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 heterocomplex Heteromer Protein × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain d; UniProt 2–161 Not recorded ATP synthase subunit alpha, mitochondrial × 3 (P19483) ATP synthase subunit beta, mitochondrial × 3 (P00829) ATP synthase subunit gamma, mitochondrial × 1 (P05631) ATP synthase subunit delta, mitochondrial × 1 (P05630) ATP synthase subunit epsilon, mitochondrial × 1 (P05632) ATPase inhibitor, mitochondrial × 1 (P01096) ATP synthase subunit O, mitochondrial × 1 (P13621) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) ATP synthase-coupling factor 6, mitochondrial × 1 (P02721) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;The sample was allowed to penetrate through the holey support and to distribute to both sides of the grid surface for ca. 15 sec. Then the grids were blotted with filter paper for 8-10 sec before blotting. Resolution 3.23 Å

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.

29 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP5H_BOVIN
Isoform
PDB entities 9
Chains and sequence ranges Author chain d; PDBConstruct 1–160; UniProt 2–161

ATP synthase-coupling factor 6, mitochondrial

OrganismNot specified

UniProt P02721

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 heterocomplex Heteromer Protein × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain h; UniProt 33–108 Not recorded ATP synthase subunit alpha, mitochondrial × 3 (P19483) ATP synthase subunit beta, mitochondrial × 3 (P00829) ATP synthase subunit gamma, mitochondrial × 1 (P05631) ATP synthase subunit delta, mitochondrial × 1 (P05630) ATP synthase subunit epsilon, mitochondrial × 1 (P05632) ATPase inhibitor, mitochondrial × 1 (P01096) ATP synthase subunit O, mitochondrial × 1 (P13621) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) ATP synthase subunit d, mitochondrial × 1 (P13620) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;The sample was allowed to penetrate through the holey support and to distribute to both sides of the grid surface for ca. 15 sec. Then the grids were blotted with filter paper for 8-10 sec before blotting. Resolution 3.23 Å

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.

30 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP5J_BOVIN
Isoform
PDB entities 10
Chains and sequence ranges Author chain h; PDBConstruct 1–76; UniProt 33–108

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 6yy0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6yy0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6yy0
Deposition date deposition_date2020-05-04
Structure title titlebovine ATP synthase F1-peripheral stalk domain, state 1
Keywords keywordsATP synthase, mitochondria, mammalian, complex, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.65
Radius of gyration Rg (electron density) rg_electron49.25
Forward intensity I(0) i02626390000.00
Molecular weight molecular_weight431520.0 kDa
Excluded volume excluded_volume542340 ų
Envelope volume envelope_volume762160 ų
Hydration-shell volume shell_volume121030 ų
Envelope diameter envelope_diameter181.2
Shell Rg shell_rg57.88
Envelope Rg envelope_rg50.11
Shape Rg shape_rg49.27
Total Rg total_rg49.45
Total atoms total_atoms61217
Residues n_residues3926
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 dmax166.4
Rg (real space) rg_real49.47
Rg uncertainty (real space) rg_real_error1.36
I(0) (real space) i0_real2.6260e+09
I(0) uncertainty (real space) i0_real_error4.5200e+07
Rg (reciprocal space) rg_reciprocal49.65
I(0) (reciprocal space) i0_reciprocal2627000000.0000
Solution quality estimate total_estimate0.8532
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary62.4
Skewness Skewness skewness0.339
Kurtosis Kurtosis kurtosis-0.093
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha524500000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.766; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.808

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

8. Citations (1)

9. Files and Curves (10)