4b2q

Model of the yeast F1Fo-ATP synthase dimer based on subtomogram average

Method: ELECTRON MICROSCOPY Dmax: 274.3 Å Quality: REASONABLE

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

ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL

OrganismNot specified

UniProt P07251

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 × 46 PDB declaration: 46-meric(46) Consistent with protein copy count Chain A; UniProt 61–545 Chain B; UniProt 60–545 Chain C; UniProt 61–545 Chain a; UniProt 61–545 Chain b; UniProt 60–545 Chain c; UniProt 61–545 Fragment:RESIDUES 61-545 Fragment:RESIDUES 60-545 ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 2 (P00830) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 4 (P00830) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 2 (P38077) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 2 (Q12165) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 2 (P21306) ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL × 20 (P61829) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 2 (P13619) ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL × 2 (P13620) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 2 (P02721) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 2 (P13621) 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

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.

51 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPA_YEAST
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–485; UniProt 61–545 Author chain C; PDBConstruct 1–485; UniProt 61–545 Author chain a; PDBConstruct 1–485; UniProt 61–545 Author chain c; PDBConstruct 1–485; UniProt 61–545 Author chain B; PDBConstruct 1–486; UniProt 60–545 Author chain b; PDBConstruct 1–486; UniProt 60–545

ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL

OrganismNot specified

UniProt P00830

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 × 46 PDB declaration: 46-meric(46) Consistent with protein copy count Chain D; UniProt 39–508 Chain E; UniProt 39–511 Chain F; UniProt 39–511 Chain d; UniProt 39–508 Chain e; UniProt 39–511 Chain f; UniProt 39–511 Fragment:RESIDUES 39-508 Fragment:RESIDUES 39-511 ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 4 (P07251) ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 2 (P07251) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 2 (P38077) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 2 (Q12165) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 2 (P21306) ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL × 20 (P61829) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 2 (P13619) ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL × 2 (P13620) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 2 (P02721) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 2 (P13621) 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

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.

51 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPB_YEAST
Isoform
PDB entities 3, 4
Chains and sequence ranges Author chain D; PDBConstruct 1–470; UniProt 39–508 Author chain d; PDBConstruct 1–470; UniProt 39–508 Author chain E; PDBConstruct 1–473; UniProt 39–511 Author chain F; PDBConstruct 1–473; UniProt 39–511 Author chain e; PDBConstruct 1–473; UniProt 39–511 Author chain f; PDBConstruct 1–473; UniProt 39–511

ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL

OrganismNot specified

UniProt P38077

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 × 46 PDB declaration: 46-meric(46) Consistent with protein copy count Chain G; UniProt 34–311 Chain g; UniProt 34–311 Fragment:RESIDUES 34-311 ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 4 (P07251) ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 2 (P07251) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 2 (P00830) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 4 (P00830) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 2 (Q12165) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 2 (P21306) ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL × 20 (P61829) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 2 (P13619) ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL × 2 (P13620) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 2 (P02721) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 2 (P13621) 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

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.

52 other PDB entries and 65 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPG_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain G; PDBConstruct 1–278; UniProt 34–311 Author chain g; PDBConstruct 1–278; UniProt 34–311

ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL

OrganismNot specified

UniProt Q12165

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 × 46 PDB declaration: 46-meric(46) Consistent with protein copy count Chain H; UniProt 29–160 Chain h; UniProt 29–160 Fragment:RESIDUES 29-160 ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 4 (P07251) ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 2 (P07251) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 2 (P00830) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 4 (P00830) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 2 (P38077) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 2 (P21306) ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL × 20 (P61829) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 2 (P13619) ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL × 2 (P13620) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 2 (P02721) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 2 (P13621) 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

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.

48 other PDB entries and 60 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPD_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain H; PDBConstruct 1–132; UniProt 29–160 Author chain h; PDBConstruct 1–132; UniProt 29–160

ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL

OrganismNot specified

UniProt P21306

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 × 46 PDB declaration: 46-meric(46) Consistent with protein copy count Chain I; UniProt 2–60 Chain i; UniProt 2–60 Fragment:RESIDUES 2-60 ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 4 (P07251) ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 2 (P07251) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 2 (P00830) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 4 (P00830) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 2 (P38077) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 2 (Q12165) ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL × 20 (P61829) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 2 (P13619) ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL × 2 (P13620) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 2 (P02721) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 2 (P13621) 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

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.

47 other PDB entries and 59 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP5E_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain I; PDBConstruct 1–59; UniProt 2–60 Author chain i; PDBConstruct 1–59; UniProt 2–60

ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL

OrganismNot specified

UniProt P61829

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 × 46 PDB declaration: 46-meric(46) Consistent with protein copy count Chain J; UniProt 1–76 Chain K; UniProt 1–76 Chain L; UniProt 1–76 Chain M; UniProt 1–76 Chain N; UniProt 1–76 Chain O; UniProt 1–76 Chain P; UniProt 1–76 Chain Q; UniProt 1–76 Chain R; UniProt 1–76 Chain S; UniProt 1–76 Chain j; UniProt 1–76 Chain k; UniProt 1–76 Chain l; UniProt 1–76 Chain m; UniProt 1–76 Chain n; UniProt 1–76 Chain o; UniProt 1–76 Chain p; UniProt 1–76 Chain q; UniProt 1–76 Chain r; UniProt 1–76 Chain s; UniProt 1–76 Not recorded ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 4 (P07251) ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 2 (P07251) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 2 (P00830) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 4 (P00830) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 2 (P38077) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 2 (Q12165) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 2 (P21306) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 2 (P13619) ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL × 2 (P13620) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 2 (P02721) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 2 (P13621) 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

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.

48 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP9_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain J; PDBConstruct 1–76; UniProt 1–76 Author chain K; PDBConstruct 1–76; UniProt 1–76 Author chain L; PDBConstruct 1–76; UniProt 1–76 Author chain M; PDBConstruct 1–76; UniProt 1–76 Author chain N; PDBConstruct 1–76; UniProt 1–76 Author chain O; PDBConstruct 1–76; UniProt 1–76 Author chain P; PDBConstruct 1–76; UniProt 1–76 Author chain Q; PDBConstruct 1–76; UniProt 1–76 Author chain R; PDBConstruct 1–76; UniProt 1–76 Author chain S; PDBConstruct 1–76; UniProt 1–76 Author chain j; PDBConstruct 1–76; UniProt 1–76 Author chain k; PDBConstruct 1–76; UniProt 1–76 Author chain l; PDBConstruct 1–76; UniProt 1–76 Author chain m; PDBConstruct 1–76; UniProt 1–76 Author chain n; PDBConstruct 1–76; UniProt 1–76 Author chain o; PDBConstruct 1–76; UniProt 1–76 Author chain p; PDBConstruct 1–76; UniProt 1–76 Author chain q; PDBConstruct 1–76; UniProt 1–76 Author chain r; PDBConstruct 1–76; UniProt 1–76 Author chain s; PDBConstruct 1–76; UniProt 1–76

ATP SYNTHASE SUBUNIT B, 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 × 46 PDB declaration: 46-meric(46) Consistent with protein copy count Chain T; UniProt 121–249 Chain t; UniProt 121–249 Fragment:RESIDUES 121-249 ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 4 (P07251) ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 2 (P07251) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 2 (P00830) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 4 (P00830) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 2 (P38077) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 2 (Q12165) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 2 (P21306) ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL × 20 (P61829) ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL × 2 (P13620) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 2 (P02721) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 2 (P13621) 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

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 9
Chains and sequence ranges Author chain T; PDBConstruct 1–129; UniProt 121–249 Author chain t; PDBConstruct 1–129; UniProt 121–249

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 × 46 PDB declaration: 46-meric(46) Consistent with protein copy count Chain U; UniProt 5–124 Chain u; UniProt 5–124 Fragment:RESIDUES 5-124 ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 4 (P07251) ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 2 (P07251) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 2 (P00830) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 4 (P00830) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 2 (P38077) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 2 (Q12165) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 2 (P21306) ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL × 20 (P61829) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 2 (P13619) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 2 (P02721) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 2 (P13621) 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

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 10
Chains and sequence ranges Author chain U; PDBConstruct 1–120; UniProt 5–124 Author chain u; PDBConstruct 1–120; UniProt 5–124

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 × 46 PDB declaration: 46-meric(46) Consistent with protein copy count Chain V; UniProt 36–101 Chain v; UniProt 36–101 Fragment:RESIDUES 36-101 ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 4 (P07251) ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 2 (P07251) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 2 (P00830) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 4 (P00830) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 2 (P38077) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 2 (Q12165) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 2 (P21306) ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL × 20 (P61829) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 2 (P13619) ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL × 2 (P13620) ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL × 2 (P13621) 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

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 11
Chains and sequence ranges Author chain V; PDBConstruct 1–66; UniProt 36–101 Author chain v; PDBConstruct 1–66; UniProt 36–101

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 × 46 PDB declaration: 46-meric(46) Consistent with protein copy count Chain W; UniProt 24–143 Chain w; UniProt 24–143 Fragment:RESIDUES 24-143 ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 4 (P07251) ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 2 (P07251) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 2 (P00830) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 4 (P00830) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 2 (P38077) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 2 (Q12165) ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 2 (P21306) ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL × 20 (P61829) ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL × 2 (P13619) ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL × 2 (P13620) ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL × 2 (P02721) 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

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 12
Chains and sequence ranges Author chain W; PDBConstruct 1–120; UniProt 24–143 Author chain w; 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 4b2q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4b2q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4b2q
Deposition date deposition_date2012-07-17
Structure title titleModel of the yeast F1Fo-ATP synthase dimer based on subtomogram average
Keywords keywordsHYDROLASE, SUBTOMOGRAM AVERAGE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron137.30
Forward intensity I(0) i012069800000.00
Molecular weight molecular_weight973790.0 kDa
Excluded volume excluded_volume1233100 ų
Envelope volume envelope_volume2370500 ų
Hydration-shell volume shell_volume142880 ų
Envelope diameter envelope_diameter402.1
Shell Rg shell_rg143.70
Envelope Rg envelope_rg125.30
Shape Rg shape_rg137.30
Total Rg total_rg137.30
Total atoms total_atoms70304
Residues n_residues9026
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 dmax274.3
Rg (real space) rg_real94.16
Rg uncertainty (real space) rg_real_error0.92
I(0) (real space) i0_real8.7960e+09
I(0) uncertainty (real space) i0_real_error1.7090e+08
Rg (reciprocal space) rg_reciprocal100.80
I(0) (reciprocal space) i0_reciprocal10590000000.0000
Solution quality estimate total_estimate0.6877
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary74.8
Skewness Skewness skewness0.426
Kurtosis Kurtosis kurtosis-0.939
Angular range angular_range— – 0.0550 −1
Current regularization parameter α current_alpha8.2200
Highest regularization parameter α highest_alpha90090000.0000
Real-space data points n_real_points12
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.025; Oscil: 0.801; Stabil: 0.529; Sysdev: 1.000; Positv: 1.000; Valcen: 0.951; Smooth: 0.000

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