6zpo

bovine ATP synthase monomer state 1 (combined)

Method: ELECTRON MICROSCOPY Dmax: 206.7 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 × 29 PDB declaration: 29-meric(29) Consistent with protein copy count Chain 8; UniProt 1–66 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 C1, mitochondrial × 8 (P32876) ATP synthase subunit O, mitochondrial × 1 (P13621) 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-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 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 4.00 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 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 × 29 PDB declaration: 29-meric(29) Consistent with protein copy count Chain A; UniProt 44–553 Chain B; UniProt 44–553 Chain C; UniProt 44–553 Not recorded ATP synthase protein 8 × 1 (P03929) 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 C1, mitochondrial × 8 (P32876) ATP synthase subunit O, mitochondrial × 1 (P13621) 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-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 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 4.00 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 2
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 × 29 PDB declaration: 29-meric(29) Consistent with protein copy count Chain D; UniProt 47–528 Chain E; UniProt 47–528 Chain F; UniProt 47–528 Not recorded ATP synthase protein 8 × 1 (P03929) 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 F(0) complex subunit C1, mitochondrial × 8 (P32876) ATP synthase subunit O, mitochondrial × 1 (P13621) 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-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 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 4.00 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 3
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

Bos taurus

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 × 29 PDB declaration: 29-meric(29) Consistent with protein copy count Chain G; UniProt 26–298 Not recorded ATP synthase protein 8 × 1 (P03929) 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 F(0) complex subunit C1, mitochondrial × 8 (P32876) ATP synthase subunit O, mitochondrial × 1 (P13621) 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-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 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 4.00 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 4
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 × 29 PDB declaration: 29-meric(29) Consistent with protein copy count Chain H; UniProt 23–168 Not recorded ATP synthase protein 8 × 1 (P03929) 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 F(0) complex subunit C1, mitochondrial × 8 (P32876) ATP synthase subunit O, mitochondrial × 1 (P13621) 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-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 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 4.00 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 5
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 × 29 PDB declaration: 29-meric(29) Consistent with protein copy count Chain I; UniProt 2–51 Not recorded ATP synthase protein 8 × 1 (P03929) 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 F(0) complex subunit C1, mitochondrial × 8 (P32876) ATP synthase subunit O, mitochondrial × 1 (P13621) 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-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 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 4.00 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 6
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 × 29 PDB declaration: 29-meric(29) Consistent with protein copy count Chain J; UniProt 26–85 Not recorded ATP synthase protein 8 × 1 (P03929) 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 F(0) complex subunit C1, mitochondrial × 8 (P32876) ATP synthase subunit O, mitochondrial × 1 (P13621) 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-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 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 4.00 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 7
Chains and sequence ranges Author chain J; PDBConstruct 1–60; UniProt 26–85

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 × 29 PDB declaration: 29-meric(29) 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 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 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-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 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 4.00 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 8
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 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 × 29 PDB declaration: 29-meric(29) Consistent with protein copy count Chain S; UniProt 24–213 Not recorded ATP synthase protein 8 × 1 (P03929) 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 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-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 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 4.00 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 9
Chains and sequence ranges Author chain S; PDBConstruct 1–190; UniProt 24–213

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 × 29 PDB declaration: 29-meric(29) Consistent with protein copy count Chain a; UniProt 1–226 Not recorded ATP synthase protein 8 × 1 (P03929) 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 C1, mitochondrial × 8 (P32876) 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 subunit e, mitochondrial × 1 (Q00361) ATP synthase subunit f, mitochondrial × 1 (Q28851) ATP synthase subunit g, mitochondrial × 1 (Q28852) ATP synthase-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 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 4.00 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 10
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 × 29 PDB declaration: 29-meric(29) Consistent with protein copy count Chain b; UniProt 43–256 Not recorded ATP synthase protein 8 × 1 (P03929) 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 C1, mitochondrial × 8 (P32876) ATP synthase subunit O, mitochondrial × 1 (P13621) 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-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 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 4.00 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 11
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 × 29 PDB declaration: 29-meric(29) Consistent with protein copy count Chain d; UniProt 2–161 Not recorded ATP synthase protein 8 × 1 (P03929) 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 C1, mitochondrial × 8 (P32876) ATP synthase subunit O, mitochondrial × 1 (P13621) 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-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 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 4.00 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 12
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 × 29 PDB declaration: 29-meric(29) Consistent with protein copy count Chain e; UniProt 2–71 Not recorded ATP synthase protein 8 × 1 (P03929) 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 C1, mitochondrial × 8 (P32876) ATP synthase subunit O, mitochondrial × 1 (P13621) 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-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 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 4.00 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 13
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 × 29 PDB declaration: 29-meric(29) Consistent with protein copy count Chain f; UniProt 2–88 Not recorded ATP synthase protein 8 × 1 (P03929) 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 C1, mitochondrial × 8 (P32876) ATP synthase subunit O, mitochondrial × 1 (P13621) 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-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 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 4.00 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 14
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 × 29 PDB declaration: 29-meric(29) Consistent with protein copy count Chain g; UniProt 2–103 Not recorded ATP synthase protein 8 × 1 (P03929) 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 C1, mitochondrial × 8 (P32876) ATP synthase subunit O, mitochondrial × 1 (P13621) 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-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP synthase membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 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 4.00 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 15
Chains and sequence ranges Author chain g; PDBConstruct 1–102; UniProt 2–103

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 × 29 PDB declaration: 29-meric(29) Consistent with protein copy count Chain h; UniProt 33–108 Not recorded ATP synthase protein 8 × 1 (P03929) 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 C1, mitochondrial × 8 (P32876) ATP synthase subunit O, mitochondrial × 1 (P13621) 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) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 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 4.00 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 16
Chains and sequence ranges Author chain h; PDBConstruct 1–76; UniProt 33–108

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 × 29 PDB declaration: 29-meric(29) Consistent with protein copy count Chain j; UniProt 1–60 Not recorded ATP synthase protein 8 × 1 (P03929) 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 C1, mitochondrial × 8 (P32876) ATP synthase subunit O, mitochondrial × 1 (P13621) 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-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase membrane subunit DAPIT, mitochondrial × 1 (Q3ZBI7) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 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 4.00 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 17
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 × 29 PDB declaration: 29-meric(29) Consistent with protein copy count Chain k; UniProt 2–58 Not recorded ATP synthase protein 8 × 1 (P03929) 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 C1, mitochondrial × 8 (P32876) ATP synthase subunit O, mitochondrial × 1 (P13621) 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-coupling factor 6, mitochondrial × 1 (P02721) ATP synthase subunit ATP5MPL, mitochondrial × 1 (P14790) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 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 4.00 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 18
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 6zpo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6zpo
Deposition date deposition_date2020-07-09
Structure title titlebovine ATP synthase monomer state 1 (combined)
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_guinier65.10
Radius of gyration Rg (electron density) rg_electron66.95
Forward intensity I(0) i04193360000.00
Molecular weight molecular_weight568040.0 kDa
Excluded volume excluded_volume720610 ų
Envelope volume envelope_volume1050600 ų
Hydration-shell volume shell_volume133200 ų
Envelope diameter envelope_diameter236.2
Shell Rg shell_rg64.97
Envelope Rg envelope_rg66.30
Shape Rg shape_rg66.92
Total Rg total_rg67.01
Total atoms total_atoms81035
Residues n_residues5142
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 dmax206.7
Rg (real space) rg_real65.72
Rg uncertainty (real space) rg_real_error1.49
I(0) (real space) i0_real4.1920e+09
I(0) uncertainty (real space) i0_real_error9.2290e+07
Rg (reciprocal space) rg_reciprocal64.46
I(0) (reciprocal space) i0_reciprocal4183000000.0000
Solution quality estimate total_estimate0.8002
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary60.3
Skewness Skewness skewness0.535
Kurtosis Kurtosis kurtosis-0.425
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0010
Highest regularization parameter α highest_alpha502900000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.790; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.036

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (24)

8. Citations (1)

9. Files and Curves (10)