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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：P32876 New Search
14PDB entries
14Biological assembly
107chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
2XND Crystal structure of bovine F1-c8 sub-complex of ATP Synthase Deposited 2010-08-02 Assembly 1 Protein heterocomplex Heteromer；Protein × 17 PDB declaration: heptadecameric（17） Consistent with protein count
Chain J 63–134（72 aa） Fragment：RESIDUES 63-134
Chain K 63–134（72 aa） Fragment：RESIDUES 63-134
Chain L 63–134（72 aa） Fragment：RESIDUES 63-134
Chain M 63–134（72 aa） Fragment：RESIDUES 63-134
Chain N 63–134（72 aa） Fragment：RESIDUES 63-134
Chain O 63–134（72 aa） Fragment：RESIDUES 63-134
Chain P 63–134（72 aa） Fragment：RESIDUES 63-134
Chain Q 63–134（72 aa） Fragment：RESIDUES 63-134
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 5 GOL GLYCEROL × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；CRYSTALS WERE GROWN UNDER OIL BY MIXING EQUAL VOLUMES OF PROTEIN (10MG/ML IN 20MM TRIS PH 8.0, 10% GLYCEROL, 1MM ADP, 1MM AMP-PNP, 2MM MGSO4, 0.02% NAN3, 5.7MM TDM) AND PRECIPITANT SOLUTION (50MM HEPES PH 7.0, 14% PEG4600, 50MM K2HPO4)
Resolution 3.50 Å R-free 0.304
5ARA Bovine mitochondrial ATP synthase state 1a Deposited 2015-09-24 Assembly 1 Protein heterocomplex Heteromer；Protein × 22 PDB declaration: 22-meric（22） Consistent with protein count
Chain J 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain K 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain L 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain M 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain N 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain O 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain P 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain Q 63–134（72 aa） Fragment：UNP RESIDUES 63-134
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 22 PDB declaration: 22-meric（22） Consistent with protein count
Chain J 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain K 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain L 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain M 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain N 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain O 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain P 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain Q 63–134（72 aa） Fragment：UNP RESIDUES 63-134
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 22 PDB declaration: 22-meric（22） Consistent with protein count
Chain J 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain K 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain L 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain M 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain N 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain O 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain P 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain Q 63–134（72 aa） Fragment：UNP RESIDUES 63-134
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 22 PDB declaration: 22-meric（22） Consistent with protein count
Chain J 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain K 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain L 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain M 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain N 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain O 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain P 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain Q 63–134（72 aa） Fragment：UNP RESIDUES 63-134
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 22 PDB declaration: 22-meric（22） Consistent with protein count
Chain J 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain K 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain L 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain M 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain N 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain O 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain P 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain Q 63–134（72 aa） Fragment：UNP RESIDUES 63-134
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 22 PDB declaration: 22-meric（22） Consistent with protein count
Chain J 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain K 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain L 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain M 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain N 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain O 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain P 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain Q 63–134（72 aa） Fragment：UNP RESIDUES 63-134
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 22 PDB declaration: 22-meric（22） Consistent with protein count
Chain J 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain K 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain L 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain M 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain N 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain O 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain P 63–134（72 aa） Fragment：UNP RESIDUES 63-134
Chain Q 63–134（72 aa） Fragment：UNP RESIDUES 63-134
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
6ZBB bovine ATP synthase Fo domain Deposited 2020-06-08 Assembly 1 Protein heterocomplex Heteromer；Protein × 17 PDB declaration: heptadecameric（17） Consistent with protein count
Chain K 62–136（75 aa）
Chain L 62–136（75 aa）
Chain M 62–136（75 aa）
Chain N 62–136（75 aa）
Chain O 62–136（75 aa）
Chain P 62–136（75 aa）
Chain Q 62–136（75 aa）
Chain R 62–136（75 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) 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
6ZIQ bovine ATP synthase stator domain, state 1 Deposited 2020-06-26 Assembly 1 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: pentadecameric（15） Consistent with protein count
Chain M 62–136（75 aa）
Chain N 62–136（75 aa）
Chain O 62–136（75 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) 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
6ZPO bovine ATP synthase monomer state 1 (combined) Deposited 2020-07-09 Assembly 1 Protein heterocomplex Heteromer；Protein × 29 PDB declaration: 29-meric（29） Consistent with protein count
Chain K 62–136（75 aa）
Chain L 62–136（75 aa）
Chain M 62–136（75 aa）
Chain N 62–136（75 aa）
Chain O 62–136（75 aa）
Chain P 62–136（75 aa）
Chain Q 62–136（75 aa）
Chain R 62–136（75 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) 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
9W2R Cryo-EM structure of FoF1-ATPase monomer state 1 on the bovine heart submitochondrial particles (FoF1-1) Deposited 2025-07-28 Assembly 1 Protein heterocomplex Heteromer；Protein × 29 PDB declaration: 29-meric（29） Consistent with protein count
Chain K 62–136（75 aa）
Chain L 62–136（75 aa）
Chain M 62–136（75 aa）
Chain N 62–136（75 aa）
Chain O 62–136（75 aa）
Chain P 62–136（75 aa）
Chain Q 62–136（75 aa）
Chain R 62–136（75 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) 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 Assembly 1 Protein heterocomplex Heteromer；Protein × 29 PDB declaration: 29-meric（29） Consistent with protein count
Chain K 62–136（75 aa）
Chain L 62–136（75 aa）
Chain M 62–136（75 aa）
Chain N 62–136（75 aa）
Chain O 62–136（75 aa）
Chain P 62–136（75 aa）
Chain Q 62–136（75 aa）
Chain R 62–136（75 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.00 Å
9W2T Cryo-EM structure of Fo domain of FoF1-ATPase monomer state on the bovine heart submitochondrial particles Deposited 2025-07-28 Assembly 1 Protein heterocomplex Heteromer；Protein × 17 PDB declaration: heptadecameric（17） Consistent with protein count
Chain K 62–136（75 aa）
Chain L 62–136（75 aa）
Chain M 62–136（75 aa）
Chain N 62–136（75 aa）
Chain O 62–136（75 aa）
Chain P 62–136（75 aa）
Chain Q 62–136（75 aa）
Chain R 62–136（75 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.10 Å

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.