6ziu

bovine ATP synthase stator domain, state 3

Method: ELECTRON MICROSCOPY Dmax: 215.6 Å Quality: REASONABLE

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

ATP synthase protein 8

OrganismNot specified

UniProt P03929

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain 8; UniProt 1–66 Not recorded ATP synthase subunit a × 1 (P00847) ATP synthase subunit d, mitochondrial × 1 (P13620) ATP synthase subunit e, mitochondrial × 1 (Q00361) ATP synthase subunit f, mitochondrial × 1 (Q28851) ATP synthase subunit g, mitochondrial × 1 (Q28852) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) ATP synthase-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit O, mitochondrial × 1 (P13621) ATP synthase subunit alpha, mitochondrial × 1 (P19483) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Th sample was allowed to penetrate through the holey grid support and to distribute to both sides of the grid surface for ~15sec. Then the grids were blotted with filter paper for 8-10 sec before blotting. Resolution 6.02 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.

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP8_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain 8; PDBConstruct 1–66; UniProt 1–66

ATP synthase subunit a

OrganismNot specified

UniProt P00847

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain a; UniProt 1–226 Not recorded ATP synthase protein 8 × 1 (P03929) ATP synthase subunit d, mitochondrial × 1 (P13620) ATP synthase subunit e, mitochondrial × 1 (Q00361) ATP synthase subunit f, mitochondrial × 1 (Q28851) ATP synthase subunit g, mitochondrial × 1 (Q28852) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) ATP synthase-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit O, mitochondrial × 1 (P13621) ATP synthase subunit alpha, mitochondrial × 1 (P19483) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Th sample was allowed to penetrate through the holey grid support and to distribute to both sides of the grid surface for ~15sec. Then the grids were blotted with filter paper for 8-10 sec before blotting. Resolution 6.02 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.

25 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP6_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain a; PDBConstruct 1–226; UniProt 1–226

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain d; UniProt 2–161 Not recorded ATP synthase protein 8 × 1 (P03929) ATP synthase subunit a × 1 (P00847) ATP synthase subunit e, mitochondrial × 1 (Q00361) ATP synthase subunit f, mitochondrial × 1 (Q28851) ATP synthase subunit g, mitochondrial × 1 (Q28852) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) ATP synthase-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit O, mitochondrial × 1 (P13621) ATP synthase subunit alpha, mitochondrial × 1 (P19483) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Th sample was allowed to penetrate through the holey grid support and to distribute to both sides of the grid surface for ~15sec. Then the grids were blotted with filter paper for 8-10 sec before blotting. Resolution 6.02 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 3
Chains and sequence ranges Author chain d; PDBConstruct 1–160; UniProt 2–161

ATP synthase subunit e, mitochondrial

OrganismNot specified

UniProt Q00361

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain e; UniProt 2–71 Not recorded ATP synthase protein 8 × 1 (P03929) ATP synthase subunit a × 1 (P00847) ATP synthase subunit d, mitochondrial × 1 (P13620) ATP synthase subunit f, mitochondrial × 1 (Q28851) ATP synthase subunit g, mitochondrial × 1 (Q28852) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) ATP synthase-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit O, mitochondrial × 1 (P13621) ATP synthase subunit alpha, mitochondrial × 1 (P19483) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Th sample was allowed to penetrate through the holey grid support and to distribute to both sides of the grid surface for ~15sec. Then the grids were blotted with filter paper for 8-10 sec before blotting. Resolution 6.02 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.

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP5I_BOVIN
Isoform
PDB entities 4
Chains and sequence ranges Author chain e; PDBConstruct 1–70; UniProt 2–71

ATP synthase subunit f, mitochondrial

OrganismNot specified

UniProt Q28851

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain f; UniProt 2–88 Not recorded ATP synthase protein 8 × 1 (P03929) ATP synthase subunit a × 1 (P00847) ATP synthase subunit d, mitochondrial × 1 (P13620) ATP synthase subunit e, mitochondrial × 1 (Q00361) ATP synthase subunit g, mitochondrial × 1 (Q28852) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) ATP synthase-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit O, mitochondrial × 1 (P13621) ATP synthase subunit alpha, mitochondrial × 1 (P19483) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Th sample was allowed to penetrate through the holey grid support and to distribute to both sides of the grid surface for ~15sec. Then the grids were blotted with filter paper for 8-10 sec before blotting. Resolution 6.02 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.

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPK_BOVIN
Isoform
PDB entities 5
Chains and sequence ranges Author chain f; PDBConstruct 1–87; UniProt 2–88

ATP synthase subunit g, mitochondrial

OrganismNot specified

UniProt Q28852

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain g; UniProt 2–103 Not recorded ATP synthase protein 8 × 1 (P03929) ATP synthase subunit a × 1 (P00847) ATP synthase subunit d, mitochondrial × 1 (P13620) ATP synthase subunit e, mitochondrial × 1 (Q00361) ATP synthase subunit f, mitochondrial × 1 (Q28851) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) ATP synthase-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit O, mitochondrial × 1 (P13621) ATP synthase subunit alpha, mitochondrial × 1 (P19483) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Th sample was allowed to penetrate through the holey grid support and to distribute to both sides of the grid surface for ~15sec. Then the grids were blotted with filter paper for 8-10 sec before blotting. Resolution 6.02 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.

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP5L_BOVIN
Isoform
PDB entities 6
Chains and sequence ranges Author chain g; PDBConstruct 1–102; UniProt 2–103

ATP synthase subunit ATP5MPL, mitochondrial

OrganismNot specified

UniProt P14790

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain j; UniProt 1–60 Not recorded ATP synthase protein 8 × 1 (P03929) ATP synthase subunit a × 1 (P00847) ATP synthase subunit d, mitochondrial × 1 (P13620) ATP synthase subunit e, mitochondrial × 1 (Q00361) ATP synthase subunit f, mitochondrial × 1 (Q28851) ATP synthase subunit g, mitochondrial × 1 (Q28852) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) ATP synthase-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit O, mitochondrial × 1 (P13621) ATP synthase subunit alpha, mitochondrial × 1 (P19483) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Th sample was allowed to penetrate through the holey grid support and to distribute to both sides of the grid surface for ~15sec. Then the grids were blotted with filter paper for 8-10 sec before blotting. Resolution 6.02 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.

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP68_BOVIN
Isoform
PDB entities 7
Chains and sequence ranges Author chain j; PDBConstruct 1–60; UniProt 1–60

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain b; UniProt 43–256 Not recorded ATP synthase protein 8 × 1 (P03929) ATP synthase subunit a × 1 (P00847) ATP synthase subunit d, mitochondrial × 1 (P13620) ATP synthase subunit e, mitochondrial × 1 (Q00361) ATP synthase subunit f, mitochondrial × 1 (Q28851) ATP synthase subunit g, mitochondrial × 1 (Q28852) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit O, mitochondrial × 1 (P13621) ATP synthase subunit alpha, mitochondrial × 1 (P19483) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Th sample was allowed to penetrate through the holey grid support and to distribute to both sides of the grid surface for ~15sec. Then the grids were blotted with filter paper for 8-10 sec before blotting. Resolution 6.02 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-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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain h; UniProt 33–108 Not recorded ATP synthase protein 8 × 1 (P03929) ATP synthase subunit a × 1 (P00847) ATP synthase subunit d, mitochondrial × 1 (P13620) ATP synthase subunit e, mitochondrial × 1 (Q00361) ATP synthase subunit f, mitochondrial × 1 (Q28851) ATP synthase subunit g, mitochondrial × 1 (Q28852) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) ATP synthase subunit O, mitochondrial × 1 (P13621) ATP synthase subunit alpha, mitochondrial × 1 (P19483) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Th sample was allowed to penetrate through the holey grid support and to distribute to both sides of the grid surface for ~15sec. Then the grids were blotted with filter paper for 8-10 sec before blotting. Resolution 6.02 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 9
Chains and sequence ranges Author chain h; PDBConstruct 1–76; UniProt 33–108

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain S; UniProt 24–213 Not recorded ATP synthase protein 8 × 1 (P03929) ATP synthase subunit a × 1 (P00847) ATP synthase subunit d, mitochondrial × 1 (P13620) ATP synthase subunit e, mitochondrial × 1 (Q00361) ATP synthase subunit f, mitochondrial × 1 (Q28851) ATP synthase subunit g, mitochondrial × 1 (Q28852) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) ATP synthase-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit alpha, mitochondrial × 1 (P19483) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Th sample was allowed to penetrate through the holey grid support and to distribute to both sides of the grid surface for ~15sec. Then the grids were blotted with filter paper for 8-10 sec before blotting. Resolution 6.02 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 10
Chains and sequence ranges Author chain S; PDBConstruct 1–190; UniProt 24–213

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain C; UniProt 44–553 Not recorded ATP synthase protein 8 × 1 (P03929) ATP synthase subunit a × 1 (P00847) ATP synthase subunit d, mitochondrial × 1 (P13620) ATP synthase subunit e, mitochondrial × 1 (Q00361) ATP synthase subunit f, mitochondrial × 1 (Q28851) ATP synthase subunit g, mitochondrial × 1 (Q28852) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) ATP synthase-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit O, mitochondrial × 1 (P13621) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Th sample was allowed to penetrate through the holey grid support and to distribute to both sides of the grid surface for ~15sec. Then the grids were blotted with filter paper for 8-10 sec before blotting. Resolution 6.02 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 11
Chains and sequence ranges Author chain C; PDBConstruct 1–510; UniProt 44–553

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 6ziu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6ziu
Deposition date deposition_date2020-06-26
Structure title titlebovine ATP synthase stator domain, state 3
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_guinier75.22
Radius of gyration Rg (electron density) rg_electron76.08
Forward intensity I(0) i0213662000.00
Molecular weight molecular_weight131810.0 kDa
Excluded volume excluded_volume168760 ų
Envelope volume envelope_volume333030 ų
Hydration-shell volume shell_volume39296 ų
Envelope diameter envelope_diameter235.3
Shell Rg shell_rg65.50
Envelope Rg envelope_rg72.87
Shape Rg shape_rg75.99
Total Rg total_rg76.21
Total atoms total_atoms18919
Residues n_residues1162
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 dmax215.6
Rg (real space) rg_real76.05
Rg uncertainty (real space) rg_real_error1.81
I(0) (real space) i0_real2.1360e+08
I(0) uncertainty (real space) i0_real_error4.1820e+06
Rg (reciprocal space) rg_reciprocal71.42
I(0) (reciprocal space) i0_reciprocal211600000.0000
Solution quality estimate total_estimate0.5900
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.1
Skewness Skewness skewness0.327
Kurtosis Kurtosis kurtosis-1.238
Angular range angular_range— – 0.1050 −1
Current regularization parameter α current_alpha0.0005
Highest regularization parameter α highest_alpha7605000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.201; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.065; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)