5ara

Bovine mitochondrial ATP synthase state 1a

Method: ELECTRON MICROSCOPY Dmax: 214.3 Å Quality: REASONABLE

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

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain A; UniProt 44–553 Chain B; UniProt 44–553 Chain C; UniProt 44–553 Fragment:UNP RESIDUES 44-553 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 F(0) COMPLEX SUBUNIT B1, MITOCHONDRIAL × 1 (P13619) ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL × 1 (P13620) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 1 (P00847) 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

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 1
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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain D; UniProt 47–528 Chain E; UniProt 47–528 Chain F; UniProt 47–528 Fragment:UNP RESIDUES 47-528 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) 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-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 1 (P00847) 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

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 2
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

OrganismNot specified

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain G; UniProt 26–298 Fragment:UNP RESIDUES 26-298 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) 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-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 1 (P00847) 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

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 3
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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain H; UniProt 23–168 Fragment:UNP RESIDUES 23-168 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) 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-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 1 (P00847) 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

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 4
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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain I; UniProt 2–51 Fragment:UNP RESIDUES 2-51 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 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-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 1 (P00847) 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

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 5
Chains and sequence ranges Author chain I; PDBConstruct 1–50; UniProt 2–51

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain J; UniProt 63–134 Chain K; UniProt 63–134 Chain L; UniProt 63–134 Chain M; UniProt 63–134 Chain N; UniProt 63–134 Chain O; UniProt 63–134 Chain P; UniProt 63–134 Chain Q; UniProt 63–134 Fragment:UNP RESIDUES 63-134 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 SUBUNIT O, MITOCHONDRIAL × 1 (P13621) ATP SYNTHASE F(0) COMPLEX SUBUNIT B1, MITOCHONDRIAL × 1 (P13619) ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL × 1 (P13620) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 1 (P00847) 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

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 6
Chains and sequence ranges Author chain J; PDBConstruct 1–72; UniProt 63–134 Author chain K; PDBConstruct 1–72; UniProt 63–134 Author chain L; PDBConstruct 1–72; UniProt 63–134 Author chain M; PDBConstruct 1–72; UniProt 63–134 Author chain N; PDBConstruct 1–72; UniProt 63–134 Author chain O; PDBConstruct 1–72; UniProt 63–134 Author chain P; PDBConstruct 1–72; UniProt 63–134 Author chain Q; PDBConstruct 1–72; UniProt 63–134

ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL

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 heterocomplex Heteromer Protein × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain S; UniProt 24–213 Fragment:UNP RESIDUES 24-213 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 F(0) COMPLEX SUBUNIT B1, MITOCHONDRIAL × 1 (P13619) ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL × 1 (P13620) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 1 (P00847) 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

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 7
Chains and sequence ranges Author chain S; PDBConstruct 1–190; UniProt 24–213

ATP SYNTHASE F(0) COMPLEX SUBUNIT B1, MITOCHONDRIAL

BOS TAURUS

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain T; UniProt 76–249 Fragment:UNP RESIDUES 76-249 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 D, MITOCHONDRIAL × 1 (P13620) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 1 (P00847) 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

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

31 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AT5F1_BOVIN
Isoform
PDB entities 8
Chains and sequence ranges Author chain T; PDBConstruct 1–174; UniProt 76–249

ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL

BOS TAURUS

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain U; UniProt 2–125 Fragment:UNP RESIDUES 2-125 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 F(0) COMPLEX SUBUNIT B1, MITOCHONDRIAL × 1 (P13619) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 1 (P00847) 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

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 9
Chains and sequence ranges Author chain U; PDBConstruct 1–124; UniProt 2–125

ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL

BOS TAURUS

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain V; UniProt 32–108 Fragment:UNP RESIDUES 32-108 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 F(0) COMPLEX SUBUNIT B1, MITOCHONDRIAL × 1 (P13619) ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL × 1 (P13620) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 1 (P00847) 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

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 10
Chains and sequence ranges Author chain V; PDBConstruct 1–77; UniProt 32–108

ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain W; UniProt 10–226 Fragment:UNP RESIDUES 10-226 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 F(0) COMPLEX SUBUNIT B1, MITOCHONDRIAL × 1 (P13619) ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL × 1 (P13620) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 1 (P02721) 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

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 11
Chains and sequence ranges Author chain W; PDBConstruct 1–217; UniProt 10–226

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 5ara

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5ara
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5ara
Deposition date deposition_date2015-09-24
Structure title titleBovine mitochondrial ATP synthase state 1a
Keywords keywordsHYDROLASE, ATP SYNTHASE, ROTARY ATPASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier60.98
Radius of gyration Rg (electron density) rg_electron61.67
Forward intensity I(0) i02526010000.00
Molecular weight molecular_weight260080.0 kDa
Excluded volume excluded_volume256370 ų
Envelope volume envelope_volume715900 ų
Hydration-shell volume shell_volume104550 ų
Envelope diameter envelope_diameter217.0
Shell Rg shell_rg58.17
Envelope Rg envelope_rg58.54
Shape Rg shape_rg61.65
Total Rg total_rg61.63
Total atoms total_atoms18544
Residues n_residues4640
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 dmax214.3
Rg (real space) rg_real61.52
Rg uncertainty (real space) rg_real_error2.38
I(0) (real space) i0_real2.5260e+09
I(0) uncertainty (real space) i0_real_error5.6190e+07
Rg (reciprocal space) rg_reciprocal60.50
I(0) (reciprocal space) i0_reciprocal2522000000.0000
Solution quality estimate total_estimate0.5824
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary57.7
Skewness Skewness skewness0.559
Kurtosis Kurtosis kurtosis-0.293
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha261700000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.646; Stabil: 1.000; Sysdev: 0.025; Positv: 1.000; Valcen: 0.998; Smooth: 0.555

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