6zbb

bovine ATP synthase Fo domain

Method: ELECTRON MICROSCOPY Dmax: 119.8 Å Quality: GOOD

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain 8; UniProt 1–66 Not recorded ATP synthase F(0) complex subunit C1, mitochondrial × 8 (P32876) ATP synthase subunit a × 1 (P00847) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) 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 membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) CDL CARDIOLIPIN × 3 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 2 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 3.61 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 F(0) complex subunit C1, mitochondrial

OrganismNot specified

UniProt P32876

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain K; UniProt 62–136 Chain L; UniProt 62–136 Chain M; UniProt 62–136 Chain N; UniProt 62–136 Chain O; UniProt 62–136 Chain P; UniProt 62–136 Chain Q; UniProt 62–136 Chain R; UniProt 62–136 Non-standard monomer:Yes (specific site not provided by mmCIF) ATP synthase protein 8 × 1 (P03929) ATP synthase subunit a × 1 (P00847) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) 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 membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) CDL CARDIOLIPIN × 3 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 2 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 3.61 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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AT5G1_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain K; PDBConstruct 1–75; UniProt 62–136 Author chain L; PDBConstruct 1–75; UniProt 62–136 Author chain M; PDBConstruct 1–75; UniProt 62–136 Author chain N; PDBConstruct 1–75; UniProt 62–136 Author chain O; PDBConstruct 1–75; UniProt 62–136 Author chain P; PDBConstruct 1–75; UniProt 62–136 Author chain Q; PDBConstruct 1–75; UniProt 62–136 Author chain R; PDBConstruct 1–75; UniProt 62–136

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain a; UniProt 1–226 Not recorded ATP synthase protein 8 × 1 (P03929) ATP synthase F(0) complex subunit C1, mitochondrial × 8 (P32876) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) 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 membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) CDL CARDIOLIPIN × 3 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 2 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 3.61 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 3
Chains and sequence ranges Author chain a; PDBConstruct 1–226; UniProt 1–226

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain b; UniProt 43–256 Not recorded ATP synthase protein 8 × 1 (P03929) ATP synthase F(0) complex subunit C1, mitochondrial × 8 (P32876) 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 membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) CDL CARDIOLIPIN × 3 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 2 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 3.61 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 4
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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain d; UniProt 2–161 Not recorded ATP synthase protein 8 × 1 (P03929) ATP synthase F(0) complex subunit C1, mitochondrial × 8 (P32876) ATP synthase subunit a × 1 (P00847) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) 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 membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) CDL CARDIOLIPIN × 3 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 2 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 3.61 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 5
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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain e; UniProt 2–71 Not recorded ATP synthase protein 8 × 1 (P03929) ATP synthase F(0) complex subunit C1, mitochondrial × 8 (P32876) ATP synthase subunit a × 1 (P00847) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) 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 membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) CDL CARDIOLIPIN × 3 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 2 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 3.61 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 6
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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain f; UniProt 2–88 Not recorded ATP synthase protein 8 × 1 (P03929) ATP synthase F(0) complex subunit C1, mitochondrial × 8 (P32876) ATP synthase subunit a × 1 (P00847) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) 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 membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) CDL CARDIOLIPIN × 3 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 2 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 3.61 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 7
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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain g; UniProt 2–103 Not recorded ATP synthase protein 8 × 1 (P03929) ATP synthase F(0) complex subunit C1, mitochondrial × 8 (P32876) ATP synthase subunit a × 1 (P00847) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) 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 membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) CDL CARDIOLIPIN × 3 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 2 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 3.61 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 8
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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain j; UniProt 1–60 Not recorded ATP synthase protein 8 × 1 (P03929) ATP synthase F(0) complex subunit C1, mitochondrial × 8 (P32876) ATP synthase subunit a × 1 (P00847) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) 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 membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) CDL CARDIOLIPIN × 3 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 2 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 3.61 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 9
Chains and sequence ranges Author chain j; PDBConstruct 1–60; UniProt 1–60

ATP synthase membrane subunit DAPIT, mitochondrial

OrganismNot specified

UniProt Q3ZBI7

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain k; UniProt 2–58 Not recorded ATP synthase protein 8 × 1 (P03929) ATP synthase F(0) complex subunit C1, mitochondrial × 8 (P32876) ATP synthase subunit a × 1 (P00847) ATP synthase F(0) complex subunit B1, mitochondrial × 1 (P13619) 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) CDL CARDIOLIPIN × 3 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 2 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 3.61 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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPMD_BOVIN
Isoform
PDB entities 10
Chains and sequence ranges Author chain k; PDBConstruct 1–57; UniProt 2–58

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 6zbb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6zbb
Deposition date deposition_date2020-06-08
Structure title titlebovine ATP synthase Fo domain
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_guinier36.85
Radius of gyration Rg (electron density) rg_electron36.07
Forward intensity I(0) i0264991000.00
Molecular weight molecular_weight148990.0 kDa
Excluded volume excluded_volume193930 ų
Envelope volume envelope_volume247600 ų
Hydration-shell volume shell_volume56396 ų
Envelope diameter envelope_diameter122.7
Shell Rg shell_rg42.97
Envelope Rg envelope_rg36.23
Shape Rg shape_rg36.07
Total Rg total_rg36.58
Total atoms total_atoms21505
Residues n_residues1320
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 dmax119.8
Rg (real space) rg_real36.80
Rg uncertainty (real space) rg_real_error0.94
I(0) (real space) i0_real2.6500e+08
I(0) uncertainty (real space) i0_real_error4.8430e+06
Rg (reciprocal space) rg_reciprocal36.83
I(0) (reciprocal space) i0_reciprocal265000000.0000
Solution quality estimate total_estimate0.8902
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary41.8
Skewness Skewness skewness0.292
Kurtosis Kurtosis kurtosis-0.416
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha38850000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.906; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.853

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6zbbQ00
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)