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2bo5

Bovine oligomycin sensitivity conferral protein N-terminal domain

Method: SOLUTION NMR Dmax: 41.1 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ATP SYNTHASE OLIGOMYCIN SENSITIVITY CONFERRAL PROTEIN

BOS TAURUS

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 24–143 Fragment：N-TERMINAL DOMAIN, RESIDUES 24-143 No other associated polymer SOLUTION NMR NMR measurement conditions：pH 6.5；300 K；Ionic strength (raw mmCIF value) 0.5M NACL, 20MM SODIUM PHOSPHATE；Pressure 1.0 NMR sample composition：7% D2O, 93%H2O Resolution not provided

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.

Other PDB Difference from Current Entry 2BO5 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2JMX OSCP-NT (1-120) in complex with N-terminal (1-25) alpha subunit from F1-ATPase Deposited 2006-12-12 Different construct Different oligomeric state Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 24–143（120 aa） Fragment：ATP synthase O subunit, residues 1-120
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；300 K；Ionic strength (raw mmCIF value) 0.5；Pressure ambient
NMR sample composition 0.5 mM [U-99% 13C, U-99% 15N] oscp-nt, 1.5 mM alpha-nt, 20 mM sodium phosphate, pH 6.5, 0.5 M NaCl, 0.001% PMSF 95% H2O, 5% D2O | 95% H2O/5% D2O
Resolution not provided
2WSS The structure of the membrane extrinsic region of bovine ATP synthase Deposited 2009-09-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 13 PDB declaration: tridecameric
Chain S 24–213（190 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；MICROBATCH UNDER OIL
Resolution 3.20 Å R-free 0.271
2WSS The structure of the membrane extrinsic region of bovine ATP synthase Deposited 2009-09-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain W 24–213（190 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；MICROBATCH UNDER OIL
Resolution 3.20 Å R-free 0.271
4B2Q Model of the yeast F1Fo-ATP synthase dimer based on subtomogram average Deposited 2012-07-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 46 PDB declaration: 46-meric
Chain W 24–143（120 aa） Fragment：RESIDUES 24-143
Chain w 24–143（120 aa） Fragment：RESIDUES 24-143
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 4 ELECTRON MICROSCOPY
cryo-EM buffer 250MM TREHALOSE 10NM TRIS- HCL PH7.4；pH 7.4；250MM TREHALOSE 10NM TRIS- HCL PH7.4
cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, TEMPERATURE- 100, INSTRUMENT- HOMEMADE PLUNGER, METHOD- SINGLE SIDE MANUAL BLOTTING FOR 5 SECONDS.,
Resolution 37.00 Å
5ARA Bovine mitochondrial ATP synthase state 1a Deposited 2015-09-24 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 22 PDB declaration: 22-meric
Chain S 24–213（190 aa） Fragment：UNP RESIDUES 24-213
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 MM TRIS-HCL, 100 MM NACL, DODECYLMALTOSIDE, 2 MM ATP, 0.02% (WT/V) NAN3；pH 7.2；20 MM TRIS-HCL, 100 MM NACL, DODECYLMALTOSIDE, 2 MM ATP, 0.02% (WT/V) NAN3
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；VITRIFICATION 1 -- CRYOGEN- ETHANE-PROPANE MIXTURE, HUMIDITY- 100, INSTRUMENT- FEI VITROBOT MARK III, METHOD- BLOT FOR 27 SECONDS BEFORE PLUNGING,
Resolution 7.40 Å
5ARE Bovine mitochondrial ATP synthase state 1b Deposited 2015-09-24 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 22 PDB declaration: 22-meric
Chain S 24–213（190 aa） Fragment：UNP RESIDUES 24-213
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 MM TRIS-HCL, 100 MM NACL, 10% (V/V) DODECYLMALTOSIDE, 2 MM ATP, 0.02% (WT/V) NAN3；pH 7.2；20 MM TRIS-HCL, 100 MM NACL, 10% (V/V) DODECYLMALTOSIDE, 2 MM ATP, 0.02% (WT/V) NAN3
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；VITRIFICATION 1 -- CRYOGEN- ETHANE-PROPANE MIXTURE, HUMIDITY- 100, INSTRUMENT- FEI VITROBOT MARK III, METHOD- BLOT FOR 27 SECONDS BEFORE PLUNGING,
Resolution 6.70 Å
5ARH Bovine mitochondrial ATP synthase state 2a Deposited 2015-09-24 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 22 PDB declaration: 22-meric
Chain S 24–213（190 aa） Fragment：UNP RESIDUES 24-213
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 MM TRIS-HCL, 100 MM NACL, 10% (V/V) DODECYLMALTOSIDE, 2 MM ATP, 0.02% (WT/V) NAN3；pH 7.2；20 MM TRIS-HCL, 100 MM NACL, 10% (V/V) DODECYLMALTOSIDE, 2 MM ATP, 0.02% (WT/V) NAN3
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；VITRIFICATION 1 -- CRYOGEN- ETHANE-PROPANE MIXTURE, HUMIDITY- 100, INSTRUMENT- FEI VITROBOT MARK III, METHOD- BLOT FOR 27 SECONDS BEFORE PLUNGING,
Resolution 7.20 Å
5ARI Bovine mitochondrial ATP synthase state 2b Deposited 2015-09-24 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 22 PDB declaration: 22-meric
Chain S 24–213（190 aa） Fragment：UNP RESIDUES 24-213
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 MM TRIS-HCL, 100 MM NACL, 10% (V/V) DODECYLMALTOSIDE, 2 MM ATP, 0.02% (WT/V) NAN3；pH 7.2；20 MM TRIS-HCL, 100 MM NACL, 10% (V/V) DODECYLMALTOSIDE, 2 MM ATP, 0.02% (WT/V) NAN3
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；VITRIFICATION 1 -- CRYOGEN- ETHANE-PROPANE MIXTURE, HUMIDITY- 100, INSTRUMENT- FEI VITROBOT MARK III, METHOD- BLOT FOR 27 SECONDS BEFORE PLUNGING,
Resolution 7.40 Å
5FIJ Bovine mitochondrial ATP synthase state 2c Deposited 2015-09-28 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 22 PDB declaration: 22-meric
Chain S 24–213（190 aa） Fragment：UNP RESIDUES 24-213
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 MM TRIS-HCL, 100 MM NACL, 10% (V/V) DODECYLMALTOSIDE, 2 MM ATP, 0.02% (WT/V) NAN3；pH 7.2；20 MM TRIS-HCL, 100 MM NACL, 10% (V/V) DODECYLMALTOSIDE, 2 MM ATP, 0.02% (WT/V) NAN3
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；VITRIFICATION 1 -- CRYOGEN- ETHANE-PROPANE MIXTURE, HUMIDITY- 100, INSTRUMENT- FEI VITROBOT MARK III, METHOD- BLOT FOR 27 SECONDS BEFORE PLUNGING,
Resolution 7.40 Å
5FIK Bovine mitochondrial ATP synthase state 3a Deposited 2015-09-28 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 22 PDB declaration: 22-meric
Chain S 24–213（190 aa） Fragment：UNP RESIDUES 24-213
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 MM TRIS-HCL, 100 MM NACL, 10% (V/V) DODECYLMALTOSIDE, 2 MM ATP, 0.02% (WT/V) NAN3；pH 7.2；20 MM TRIS-HCL, 100 MM NACL, 10% (V/V) DODECYLMALTOSIDE, 2 MM ATP, 0.02% (WT/V) NAN3
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；VITRIFICATION 1 -- CRYOGEN- ETHANE-PROPANE MIXTURE, HUMIDITY- 100, INSTRUMENT- FEI VITROBOT MARK III, METHOD- BLOT FOR 27 SECONDS BEFORE PLUNGING,
Resolution 6.40 Å
5FIL Bovine mitochondrial ATP synthase state 3b Deposited 2015-09-28 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 22 PDB declaration: 22-meric
Chain S 24–213（190 aa） Fragment：UNP RESIDUES 24-213
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 MM TRIS-HCL, 100 MM NACL, 10% (V/V) GLYCEROL, 0.05% (WT/V) DODECYLMALTOSIDE, 2 MM ATP, 0.02% (WT/V) NAN3；pH 7.2；20 MM TRIS-HCL, 100 MM NACL, 10% (V/V) GLYCEROL, 0.05% (WT/V) DODECYLMALTOSIDE, 2 MM ATP, 0.02% (WT/V) NAN3
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；VITRIFICATION 1 -- CRYOGEN- ETHANE-PROPANE MIXTURE, HUMIDITY- 100, INSTRUMENT- FEI VITROBOT MARK III, METHOD- BLOT FOR 27 SECONDS BEFORE PLUNGING,
Resolution 7.10 Å
6YY0 bovine ATP synthase F1-peripheral stalk domain, state 1 Deposited 2020-05-04 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric
Chain S 24–213（190 aa）
Not recorded 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
6Z1R bovine ATP synthase F1-peripheral stalk domain, state 2 Deposited 2020-05-14 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 21 PDB declaration: 21-meric
Chain S 24–213（190 aa）
Not recorded 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 3.29 Å
6Z1U bovine ATP synthase F1c8-peripheral stalk domain, state 3 Deposited 2020-05-14 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 21 PDB declaration: 21-meric
Chain S 24–213（190 aa）
Not recorded 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 3.47 Å
6ZIQ bovine ATP synthase stator domain, state 1 Deposited 2020-06-26 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: pentadecameric
Chain S 24–213（190 aa）
Not recorded No recorded non-water small molecule 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 4.33 Å
6ZIT bovine ATP synthase Stator domain, state 2 Deposited 2020-06-26 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: pentadecameric
Chain S 24–213（190 aa）
Not recorded No recorded non-water small molecule 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 3.49 Å
6ZIU bovine ATP synthase stator domain, state 3 Deposited 2020-06-26 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 11 PDB declaration: undecameric
Chain S 24–213（190 aa）
Not recorded No recorded non-water small molecule 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
6ZPO bovine ATP synthase monomer state 1 (combined) Deposited 2020-07-09 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 29 PDB declaration: 29-meric
Chain S 24–213（190 aa）
Not recorded 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
6ZQM bovine ATP synthase monomer state 2 (combined) Deposited 2020-07-10 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 29 PDB declaration: 29-meric
Chain S 24–213（190 aa）
Not recorded 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 3.29 Å
6ZQN bovine ATP synthase monomer state 3 (combined) Deposited 2020-07-10 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 29 PDB declaration: 29-meric
Chain S 24–213（190 aa）
Not recorded 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
7AJB bovine ATP synthase dimer state1:state1 Deposited 2020-09-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric
Chain AS 24–213（190 aa）
Chain S 24–213（190 aa）
Not recorded CDL CARDIOLIPIN × 6 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 9.20 Å
7AJC bovine ATP synthase dimer state1:state2 Deposited 2020-09-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric
Chain AS 24–213（190 aa）
Chain S 24–213（190 aa）
Not recorded CDL CARDIOLIPIN × 6 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 11.90 Å
7AJD bovine ATP synthase dimer state1:state3 Deposited 2020-09-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric
Chain AS 24–213（190 aa）
Chain S 24–213（190 aa）
Not recorded CDL CARDIOLIPIN × 6 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 9.00 Å
7AJE bovine ATP synthase dimer state2:state1 Deposited 2020-09-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric
Chain AS 24–213（190 aa）
Chain S 24–213（190 aa）
Not recorded CDL CARDIOLIPIN × 6 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 9.40 Å
7AJF bovine ATP synthase dimer state2:state2 Deposited 2020-09-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric
Chain AS 24–213（190 aa）
Chain S 24–213（190 aa）
Not recorded CDL CARDIOLIPIN × 6 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 8.45 Å
7AJG bovine ATP synthase dimer state2:state3 Deposited 2020-09-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric
Chain AS 24–213（190 aa）
Chain S 24–213（190 aa）
Not recorded CDL CARDIOLIPIN × 6 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 10.70 Å
7AJH bovine ATP synthase dimer state3:state1 Deposited 2020-09-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric
Chain AS 24–213（190 aa）
Chain S 24–213（190 aa）
Not recorded CDL CARDIOLIPIN × 6 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 9.70 Å
7AJI bovine ATP synthase dimer state3:state2 Deposited 2020-09-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric
Chain AS 24–213（190 aa）
Chain S 24–213（190 aa）
Not recorded CDL CARDIOLIPIN × 6 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 11.40 Å
7AJJ bovine ATP synthase dimer state3:state3 Deposited 2020-09-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric
Chain AS 24–213（190 aa）
Chain S 24–213（190 aa）
Not recorded CDL CARDIOLIPIN × 6 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 13.10 Å
9W2R Cryo-EM structure of FoF1-ATPase monomer state 1 on the bovine heart submitochondrial particles (FoF1-1) Deposited 2025-07-28 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 29 PDB declaration: 29-meric
Chain S 24–213（190 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
9W2S Cryo-EM structure of FoF1-ATPase monomer state 3 on the bovine heart submitochondrial particles (FoF1-2) Deposited 2025-07-28 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 29 PDB declaration: 29-meric
Chain S 24–213（190 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.00 Å

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 1
Chains and sequence ranges Author chain A； PDBConstruct 1–120； UniProt 24–143

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 2bo5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2bo5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2bo5
Deposition date deposition_date2005-04-07
Structure title titleBovine oligomycin sensitivity conferral protein N-terminal domain
Keywords keywords;ATP SYNTHASE, PERIPHERAL STALK, OSCP, ALPHA-SUBUNIT, BETA-SUBUNIT, PROTEIN-PROTEIN INTERACTIONS, CHEMICAL SHIFT PERTURBATIONS, CHEMICAL SHIFT MAPPING, TITRATION, BINDING INTERFACE, CF(1), HYDROGEN ION TRANSPORT, HYDROLASE, ION TRANSPORT, MITOCHONDRION, TRANSIT PEPTIDE, TRANSPORT ;; HYDROLASE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier15.50 Å
Radius of gyration Rg (electron density) rg_electron15.74 Å
Forward intensity I(0) i04283830000.00
Molecular weight molecular_weight582150.0 kDa
Excluded volume excluded_volume741000 ų
Envelope volume envelope_volume64063 ų
Hydration-shell volume shell_volume23409 ų
Envelope diameter envelope_diameter73.4 Å
Shell Rg shell_rg30.41 Å
Envelope Rg envelope_rg24.23 Å
Shape Rg shape_rg15.71 Å
Total Rg total_rg16.06 Å
Total atoms total_atoms84128
Residues n_residues5280
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax41.1 Å
Rg (real space) rg_real14.64 Å
Rg uncertainty (real space) rg_real_error0.05 Å
I(0) (real space) i0_real4.0800e+09
I(0) uncertainty (real space) i0_real_error3.0940e+07
Rg (reciprocal space) rg_reciprocal15.58 Å
I(0) (reciprocal space) i0_reciprocal4284000000.0000
Solution quality estimate total_estimate0.6804
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary16.6 Å
Skewness Skewness skewness0.281
Kurtosis Kurtosis kurtosis-0.341
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha3.9510
Highest regularization parameter α highest_alpha250900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.003; Oscil: 0.969; Stabil: 0.981; Sysdev: 0.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2bo5A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology520 — Peroxidase; domain 1
Homologous superfamily homologous superfamily20 — N-terminal domain of the delta subunit of the F1F0-ATP synthase
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8. Citations (1)

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9. Files and Curves (10)