8fkj

Yeast ATP Synthase in conformation-3, at pH 6

Method: ELECTRON MICROSCOPY Dmax: 225.2 Å Quality: GOOD

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

ATP synthase subunit 5, mitochondrial

OrganismNot specified

UniProt A0A6A5Q1Y3

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain Y; UniProt 24–189 Not recorded ATP synthase subunit alpha × 3 (A0A6A5Q4L9) ATP synthase subunit beta × 3 (A0A6A5PX46) ATP synthase subunit 9, mitochondrial × 10 (A0A0G3F489) ATP synthase subunit 4, mitochondrial × 1 (P05626) ATP synthase subunit d, mitochondrial × 1 (P30902) ATP synthase subunit H, mitochondrial × 1 (Q12349) ATP synthase subunit f, mitochondrial × 1 (Q06405) ATP synthase protein 8 × 1 (A0A0G3F1I9) ATP synthase subunit a × 1 (A0A0H3WKN0) ATP18 isoform 1 × 1 (A0A6A5PRS1) ATP synthase subunit gamma × 1 (A0A6A5Q493) ATP synthase subunit delta, mitochondrial × 1 (Q12165) ATP synthase subunit epsilon, mitochondrial × 1 (P21306) ELECTRON MICROSCOPY cryo-EM buffer:pH 6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5Q1Y3_YEASX
Isoform
PDB entities 1
Chains and sequence ranges Author chain Y; PDBConstruct 1–166; UniProt 24–189

ATP synthase subunit alpha

OrganismNot specified

UniProt A0A6A5Q4L9

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain A; UniProt 39–545 Chain B; UniProt 39–545 Chain C; UniProt 39–545 Not recorded ATP synthase subunit 5, mitochondrial × 1 (A0A6A5Q1Y3) ATP synthase subunit beta × 3 (A0A6A5PX46) ATP synthase subunit 9, mitochondrial × 10 (A0A0G3F489) ATP synthase subunit 4, mitochondrial × 1 (P05626) ATP synthase subunit d, mitochondrial × 1 (P30902) ATP synthase subunit H, mitochondrial × 1 (Q12349) ATP synthase subunit f, mitochondrial × 1 (Q06405) ATP synthase protein 8 × 1 (A0A0G3F1I9) ATP synthase subunit a × 1 (A0A0H3WKN0) ATP18 isoform 1 × 1 (A0A6A5PRS1) ATP synthase subunit gamma × 1 (A0A6A5Q493) ATP synthase subunit delta, mitochondrial × 1 (Q12165) ATP synthase subunit epsilon, mitochondrial × 1 (P21306) ELECTRON MICROSCOPY cryo-EM buffer:pH 6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5Q4L9_YEASX
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–507; UniProt 39–545 Author chain B; PDBConstruct 1–507; UniProt 39–545 Author chain C; PDBConstruct 1–507; UniProt 39–545

ATP synthase subunit beta

OrganismNot specified

UniProt A0A6A5PX46

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain D; UniProt 39–511 Chain E; UniProt 39–511 Chain F; UniProt 39–511 Not recorded ATP synthase subunit 5, mitochondrial × 1 (A0A6A5Q1Y3) ATP synthase subunit alpha × 3 (A0A6A5Q4L9) ATP synthase subunit 9, mitochondrial × 10 (A0A0G3F489) ATP synthase subunit 4, mitochondrial × 1 (P05626) ATP synthase subunit d, mitochondrial × 1 (P30902) ATP synthase subunit H, mitochondrial × 1 (Q12349) ATP synthase subunit f, mitochondrial × 1 (Q06405) ATP synthase protein 8 × 1 (A0A0G3F1I9) ATP synthase subunit a × 1 (A0A0H3WKN0) ATP18 isoform 1 × 1 (A0A6A5PRS1) ATP synthase subunit gamma × 1 (A0A6A5Q493) ATP synthase subunit delta, mitochondrial × 1 (Q12165) ATP synthase subunit epsilon, mitochondrial × 1 (P21306) ELECTRON MICROSCOPY cryo-EM buffer:pH 6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5PX46_YEASX
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; 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 9, mitochondrial

OrganismNot specified

UniProt A0A0G3F489

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain K; UniProt 2–75 Chain L; UniProt 2–75 Chain M; UniProt 2–75 Chain N; UniProt 2–75 Chain O; UniProt 2–75 Chain P; UniProt 2–75 Chain Q; UniProt 2–75 Chain R; UniProt 2–75 Chain S; UniProt 2–75 Chain T; UniProt 2–75 Not recorded ATP synthase subunit 5, mitochondrial × 1 (A0A6A5Q1Y3) ATP synthase subunit alpha × 3 (A0A6A5Q4L9) ATP synthase subunit beta × 3 (A0A6A5PX46) ATP synthase subunit 4, mitochondrial × 1 (P05626) ATP synthase subunit d, mitochondrial × 1 (P30902) ATP synthase subunit H, mitochondrial × 1 (Q12349) ATP synthase subunit f, mitochondrial × 1 (Q06405) ATP synthase protein 8 × 1 (A0A0G3F1I9) ATP synthase subunit a × 1 (A0A0H3WKN0) ATP18 isoform 1 × 1 (A0A6A5PRS1) ATP synthase subunit gamma × 1 (A0A6A5Q493) ATP synthase subunit delta, mitochondrial × 1 (Q12165) ATP synthase subunit epsilon, mitochondrial × 1 (P21306) ELECTRON MICROSCOPY cryo-EM buffer:pH 6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0G3F489_YEASX
Isoform
PDB entities 4
Chains and sequence ranges Author chain K; PDBConstruct 1–74; UniProt 2–75 Author chain L; PDBConstruct 1–74; UniProt 2–75 Author chain M; PDBConstruct 1–74; UniProt 2–75 Author chain N; PDBConstruct 1–74; UniProt 2–75 Author chain O; PDBConstruct 1–74; UniProt 2–75 Author chain P; PDBConstruct 1–74; UniProt 2–75 Author chain Q; PDBConstruct 1–74; UniProt 2–75 Author chain R; PDBConstruct 1–74; UniProt 2–75 Author chain S; PDBConstruct 1–74; UniProt 2–75 Author chain T; PDBConstruct 1–74; UniProt 2–75

ATP synthase subunit 4, mitochondrial

OrganismNot specified

UniProt P05626

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain Z; UniProt 88–242 Not recorded ATP synthase subunit 5, mitochondrial × 1 (A0A6A5Q1Y3) ATP synthase subunit alpha × 3 (A0A6A5Q4L9) ATP synthase subunit beta × 3 (A0A6A5PX46) ATP synthase subunit 9, mitochondrial × 10 (A0A0G3F489) ATP synthase subunit d, mitochondrial × 1 (P30902) ATP synthase subunit H, mitochondrial × 1 (Q12349) ATP synthase subunit f, mitochondrial × 1 (Q06405) ATP synthase protein 8 × 1 (A0A0G3F1I9) ATP synthase subunit a × 1 (A0A0H3WKN0) ATP18 isoform 1 × 1 (A0A6A5PRS1) ATP synthase subunit gamma × 1 (A0A6A5Q493) ATP synthase subunit delta, mitochondrial × 1 (Q12165) ATP synthase subunit epsilon, mitochondrial × 1 (P21306) ELECTRON MICROSCOPY cryo-EM buffer:pH 6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

40 other PDB entries and 40 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPF_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain Z; PDBConstruct 1–155; UniProt 88–242

ATP synthase subunit d, mitochondrial

OrganismNot specified

UniProt P30902

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain 7; UniProt 4–174 Not recorded ATP synthase subunit 5, mitochondrial × 1 (A0A6A5Q1Y3) ATP synthase subunit alpha × 3 (A0A6A5Q4L9) ATP synthase subunit beta × 3 (A0A6A5PX46) ATP synthase subunit 9, mitochondrial × 10 (A0A0G3F489) ATP synthase subunit 4, mitochondrial × 1 (P05626) ATP synthase subunit H, mitochondrial × 1 (Q12349) ATP synthase subunit f, mitochondrial × 1 (Q06405) ATP synthase protein 8 × 1 (A0A0G3F1I9) ATP synthase subunit a × 1 (A0A0H3WKN0) ATP18 isoform 1 × 1 (A0A6A5PRS1) ATP synthase subunit gamma × 1 (A0A6A5Q493) ATP synthase subunit delta, mitochondrial × 1 (Q12165) ATP synthase subunit epsilon, mitochondrial × 1 (P21306) ELECTRON MICROSCOPY cryo-EM buffer:pH 6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

41 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP7_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain 7; PDBConstruct 1–171; UniProt 4–174

ATP synthase subunit H, mitochondrial

OrganismNot specified

UniProt Q12349

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain 6; UniProt 36–124 Not recorded ATP synthase subunit 5, mitochondrial × 1 (A0A6A5Q1Y3) ATP synthase subunit alpha × 3 (A0A6A5Q4L9) ATP synthase subunit beta × 3 (A0A6A5PX46) ATP synthase subunit 9, mitochondrial × 10 (A0A0G3F489) ATP synthase subunit 4, mitochondrial × 1 (P05626) ATP synthase subunit d, mitochondrial × 1 (P30902) ATP synthase subunit f, mitochondrial × 1 (Q06405) ATP synthase protein 8 × 1 (A0A0G3F1I9) ATP synthase subunit a × 1 (A0A0H3WKN0) ATP18 isoform 1 × 1 (A0A6A5PRS1) ATP synthase subunit gamma × 1 (A0A6A5Q493) ATP synthase subunit delta, mitochondrial × 1 (Q12165) ATP synthase subunit epsilon, mitochondrial × 1 (P21306) ELECTRON MICROSCOPY cryo-EM buffer:pH 6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

36 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP14_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain 6; PDBConstruct 1–89; UniProt 36–124

ATP synthase subunit f, mitochondrial

OrganismNot specified

UniProt Q06405

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain U; UniProt 7–91 Not recorded ATP synthase subunit 5, mitochondrial × 1 (A0A6A5Q1Y3) ATP synthase subunit alpha × 3 (A0A6A5Q4L9) ATP synthase subunit beta × 3 (A0A6A5PX46) ATP synthase subunit 9, mitochondrial × 10 (A0A0G3F489) ATP synthase subunit 4, mitochondrial × 1 (P05626) ATP synthase subunit d, mitochondrial × 1 (P30902) ATP synthase subunit H, mitochondrial × 1 (Q12349) ATP synthase protein 8 × 1 (A0A0G3F1I9) ATP synthase subunit a × 1 (A0A0H3WKN0) ATP18 isoform 1 × 1 (A0A6A5PRS1) ATP synthase subunit gamma × 1 (A0A6A5Q493) ATP synthase subunit delta, mitochondrial × 1 (Q12165) ATP synthase subunit epsilon, mitochondrial × 1 (P21306) ELECTRON MICROSCOPY cryo-EM buffer:pH 6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

41 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPK_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain U; PDBConstruct 1–85; UniProt 7–91

ATP synthase protein 8

OrganismNot specified

UniProt A0A0G3F1I9

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain 8; UniProt 7–47 Not recorded ATP synthase subunit 5, mitochondrial × 1 (A0A6A5Q1Y3) ATP synthase subunit alpha × 3 (A0A6A5Q4L9) ATP synthase subunit beta × 3 (A0A6A5PX46) ATP synthase subunit 9, mitochondrial × 10 (A0A0G3F489) ATP synthase subunit 4, mitochondrial × 1 (P05626) ATP synthase subunit d, mitochondrial × 1 (P30902) ATP synthase subunit H, mitochondrial × 1 (Q12349) ATP synthase subunit f, mitochondrial × 1 (Q06405) ATP synthase subunit a × 1 (A0A0H3WKN0) ATP18 isoform 1 × 1 (A0A6A5PRS1) ATP synthase subunit gamma × 1 (A0A6A5Q493) ATP synthase subunit delta, mitochondrial × 1 (Q12165) ATP synthase subunit epsilon, mitochondrial × 1 (P21306) ELECTRON MICROSCOPY cryo-EM buffer:pH 6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0G3F1I9_YEASX
Isoform
PDB entities 9
Chains and sequence ranges Author chain 8; PDBConstruct 1–41; UniProt 7–47

ATP synthase subunit a

OrganismNot specified

UniProt A0A0H3WKN0

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain X; UniProt 36–259 Not recorded ATP synthase subunit 5, mitochondrial × 1 (A0A6A5Q1Y3) ATP synthase subunit alpha × 3 (A0A6A5Q4L9) ATP synthase subunit beta × 3 (A0A6A5PX46) ATP synthase subunit 9, mitochondrial × 10 (A0A0G3F489) ATP synthase subunit 4, mitochondrial × 1 (P05626) ATP synthase subunit d, mitochondrial × 1 (P30902) ATP synthase subunit H, mitochondrial × 1 (Q12349) ATP synthase subunit f, mitochondrial × 1 (Q06405) ATP synthase protein 8 × 1 (A0A0G3F1I9) ATP18 isoform 1 × 1 (A0A6A5PRS1) ATP synthase subunit gamma × 1 (A0A6A5Q493) ATP synthase subunit delta, mitochondrial × 1 (Q12165) ATP synthase subunit epsilon, mitochondrial × 1 (P21306) ELECTRON MICROSCOPY cryo-EM buffer:pH 6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A0H3WKN0_YEASX
Isoform
PDB entities 10
Chains and sequence ranges Author chain X; PDBConstruct 1–224; UniProt 36–259

ATP18 isoform 1

OrganismNot specified

UniProt A0A6A5PRS1

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain J; UniProt 1–37 Not recorded ATP synthase subunit 5, mitochondrial × 1 (A0A6A5Q1Y3) ATP synthase subunit alpha × 3 (A0A6A5Q4L9) ATP synthase subunit beta × 3 (A0A6A5PX46) ATP synthase subunit 9, mitochondrial × 10 (A0A0G3F489) ATP synthase subunit 4, mitochondrial × 1 (P05626) ATP synthase subunit d, mitochondrial × 1 (P30902) ATP synthase subunit H, mitochondrial × 1 (Q12349) ATP synthase subunit f, mitochondrial × 1 (Q06405) ATP synthase protein 8 × 1 (A0A0G3F1I9) ATP synthase subunit a × 1 (A0A0H3WKN0) ATP synthase subunit gamma × 1 (A0A6A5Q493) ATP synthase subunit delta, mitochondrial × 1 (Q12165) ATP synthase subunit epsilon, mitochondrial × 1 (P21306) ELECTRON MICROSCOPY cryo-EM buffer:pH 6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5PRS1_YEASX
Isoform
PDB entities 11
Chains and sequence ranges Author chain J; PDBConstruct 1–37; UniProt 1–37

ATP synthase subunit gamma

OrganismNot specified

UniProt A0A6A5Q493

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain G; UniProt 38–307 Not recorded ATP synthase subunit 5, mitochondrial × 1 (A0A6A5Q1Y3) ATP synthase subunit alpha × 3 (A0A6A5Q4L9) ATP synthase subunit beta × 3 (A0A6A5PX46) ATP synthase subunit 9, mitochondrial × 10 (A0A0G3F489) ATP synthase subunit 4, mitochondrial × 1 (P05626) ATP synthase subunit d, mitochondrial × 1 (P30902) ATP synthase subunit H, mitochondrial × 1 (Q12349) ATP synthase subunit f, mitochondrial × 1 (Q06405) ATP synthase protein 8 × 1 (A0A0G3F1I9) ATP synthase subunit a × 1 (A0A0H3WKN0) ATP18 isoform 1 × 1 (A0A6A5PRS1) ATP synthase subunit delta, mitochondrial × 1 (Q12165) ATP synthase subunit epsilon, mitochondrial × 1 (P21306) ELECTRON MICROSCOPY cryo-EM buffer:pH 6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5Q493_YEASX
Isoform
PDB entities 12
Chains and sequence ranges Author chain G; PDBConstruct 1–270; UniProt 38–307

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain H; UniProt 29–160 Not recorded ATP synthase subunit 5, mitochondrial × 1 (A0A6A5Q1Y3) ATP synthase subunit alpha × 3 (A0A6A5Q4L9) ATP synthase subunit beta × 3 (A0A6A5PX46) ATP synthase subunit 9, mitochondrial × 10 (A0A0G3F489) ATP synthase subunit 4, mitochondrial × 1 (P05626) ATP synthase subunit d, mitochondrial × 1 (P30902) ATP synthase subunit H, mitochondrial × 1 (Q12349) ATP synthase subunit f, mitochondrial × 1 (Q06405) ATP synthase protein 8 × 1 (A0A0G3F1I9) ATP synthase subunit a × 1 (A0A0H3WKN0) ATP18 isoform 1 × 1 (A0A6A5PRS1) ATP synthase subunit gamma × 1 (A0A6A5Q493) ATP synthase subunit epsilon, mitochondrial × 1 (P21306) ELECTRON MICROSCOPY cryo-EM buffer:pH 6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 13
Chains and sequence ranges 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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain I; UniProt 2–60 Not recorded ATP synthase subunit 5, mitochondrial × 1 (A0A6A5Q1Y3) ATP synthase subunit alpha × 3 (A0A6A5Q4L9) ATP synthase subunit beta × 3 (A0A6A5PX46) ATP synthase subunit 9, mitochondrial × 10 (A0A0G3F489) ATP synthase subunit 4, mitochondrial × 1 (P05626) ATP synthase subunit d, mitochondrial × 1 (P30902) ATP synthase subunit H, mitochondrial × 1 (Q12349) ATP synthase subunit f, mitochondrial × 1 (Q06405) ATP synthase protein 8 × 1 (A0A0G3F1I9) ATP synthase subunit a × 1 (A0A0H3WKN0) ATP18 isoform 1 × 1 (A0A6A5PRS1) ATP synthase subunit gamma × 1 (A0A6A5Q493) ATP synthase subunit delta, mitochondrial × 1 (Q12165) ELECTRON MICROSCOPY cryo-EM buffer:pH 6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 14
Chains and sequence ranges Author chain I; PDBConstruct 1–59; UniProt 2–60

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 8fkj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8fkj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8fkj
Deposition date deposition_date2022-12-21
Structure title titleYeast ATP Synthase in conformation-3, at pH 6
Keywords keywordsF-type, ATP Synthase, yeast, mitochondrial, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier63.37
Radius of gyration Rg (electron density) rg_electron63.89
Forward intensity I(0) i02629920000.00
Molecular weight molecular_weight350080.0 kDa
Excluded volume excluded_volume402150 ų
Envelope volume envelope_volume860080 ų
Hydration-shell volume shell_volume117210 ų
Envelope diameter envelope_diameter225.0
Shell Rg shell_rg62.63
Envelope Rg envelope_rg60.80
Shape Rg shape_rg63.87
Total Rg total_rg63.90
Total atoms total_atoms25001
Residues n_residues5088
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 dmax225.2
Rg (real space) rg_real63.80
Rg uncertainty (real space) rg_real_error3.20
I(0) (real space) i0_real2.6300e+09
I(0) uncertainty (real space) i0_real_error6.3610e+07
Rg (reciprocal space) rg_reciprocal62.95
I(0) (reciprocal space) i0_reciprocal2626000000.0000
Solution quality estimate total_estimate0.8298
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary63.0
Skewness Skewness skewness0.462
Kurtosis Kurtosis kurtosis-0.458
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha305600000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.692; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.717

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

8. Citations (1)

9. Files and Curves (10)