6cp7

Monomer yeast ATP synthase Fo reconstituted in nanodisc generated from masked refinement.

Method: ELECTRON MICROSCOPY Dmax: 125.7 Å Quality: GOOD

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

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count 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 T; UniProt 1–76 Non-standard monomer:Yes (specific site not provided by mmCIF) ATP synthase protein 8 × 1 (P00856) ATP synthase subunit a × 1 (P00854) ATP synthase subunit 4, mitochondrial × 1 (P05626) ATP synthase subunit d, mitochondrial × 1 (P30902) ATP synthase subunit f, mitochondrial × 1 (Q06405) ATP synthase subunit J, mitochondrial × 1 (P81450) ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM Tris-HCl, 150 mM NaCl, pH 8.0 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 1
Chains and sequence ranges 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 T; PDBConstruct 1–76; UniProt 1–76

ATP synthase protein 8

OrganismNot specified

UniProt P00856

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain 8; UniProt 1–48 Not recorded ATP synthase subunit 9, mitochondrial × 10 (P61829) ATP synthase subunit a × 1 (P00854) ATP synthase subunit 4, mitochondrial × 1 (P05626) ATP synthase subunit d, mitochondrial × 1 (P30902) ATP synthase subunit f, mitochondrial × 1 (Q06405) ATP synthase subunit J, mitochondrial × 1 (P81450) ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM Tris-HCl, 150 mM NaCl, pH 8.0 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

39 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP8_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain 8; PDBConstruct 1–48; UniProt 1–48

ATP synthase subunit a

OrganismNot specified

UniProt P00854

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain X; UniProt 11–259 Not recorded ATP synthase subunit 9, mitochondrial × 10 (P61829) ATP synthase protein 8 × 1 (P00856) ATP synthase subunit 4, mitochondrial × 1 (P05626) ATP synthase subunit d, mitochondrial × 1 (P30902) ATP synthase subunit f, mitochondrial × 1 (Q06405) ATP synthase subunit J, mitochondrial × 1 (P81450) ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM Tris-HCl, 150 mM NaCl, pH 8.0 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 ATP6_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain X; PDBConstruct 1–249; UniProt 11–259

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain Z; UniProt 36–244 Not recorded ATP synthase subunit 9, mitochondrial × 10 (P61829) ATP synthase protein 8 × 1 (P00856) ATP synthase subunit a × 1 (P00854) ATP synthase subunit d, mitochondrial × 1 (P30902) ATP synthase subunit f, mitochondrial × 1 (Q06405) ATP synthase subunit J, mitochondrial × 1 (P81450) ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM Tris-HCl, 150 mM NaCl, pH 8.0 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 4
Chains and sequence ranges Author chain Z; PDBConstruct 1–209; UniProt 36–244

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain 7; UniProt 2–174 Not recorded ATP synthase subunit 9, mitochondrial × 10 (P61829) ATP synthase protein 8 × 1 (P00856) ATP synthase subunit a × 1 (P00854) ATP synthase subunit 4, mitochondrial × 1 (P05626) ATP synthase subunit f, mitochondrial × 1 (Q06405) ATP synthase subunit J, mitochondrial × 1 (P81450) ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM Tris-HCl, 150 mM NaCl, pH 8.0 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 5
Chains and sequence ranges Author chain 7; PDBConstruct 1–173; UniProt 2–174

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain U; UniProt 7–101 Not recorded ATP synthase subunit 9, mitochondrial × 10 (P61829) ATP synthase protein 8 × 1 (P00856) ATP synthase subunit a × 1 (P00854) ATP synthase subunit 4, mitochondrial × 1 (P05626) ATP synthase subunit d, mitochondrial × 1 (P30902) ATP synthase subunit J, mitochondrial × 1 (P81450) ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM Tris-HCl, 150 mM NaCl, pH 8.0 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 6
Chains and sequence ranges Author chain U; PDBConstruct 1–95; UniProt 7–101

ATP synthase subunit J, mitochondrial

OrganismNot specified

UniProt P81450

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain J; UniProt 1–37 Not recorded ATP synthase subunit 9, mitochondrial × 10 (P61829) ATP synthase protein 8 × 1 (P00856) ATP synthase subunit a × 1 (P00854) ATP synthase subunit 4, mitochondrial × 1 (P05626) ATP synthase subunit d, mitochondrial × 1 (P30902) ATP synthase subunit f, mitochondrial × 1 (Q06405) ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM Tris-HCl, 150 mM NaCl, pH 8.0 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

39 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP18_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain J; PDBConstruct 1–37; UniProt 1–37

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 6cp7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6cp7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6cp7
Deposition date deposition_date2018-03-13
Structure title titleMonomer yeast ATP synthase Fo reconstituted in nanodisc generated from masked refinement.
Keywords keywordsATP synthase, BIOSYNTHETIC PROTEIN; BIOSYNTHETIC PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.00
Radius of gyration Rg (electron density) rg_electron33.30
Forward intensity I(0) i0200964000.00
Molecular weight molecular_weight129890.0 kDa
Excluded volume excluded_volume169520 ų
Envelope volume envelope_volume211310 ų
Hydration-shell volume shell_volume52105 ų
Envelope diameter envelope_diameter137.2
Shell Rg shell_rg40.66
Envelope Rg envelope_rg33.75
Shape Rg shape_rg33.31
Total Rg total_rg33.88
Total atoms total_atoms9164
Residues n_residues1224
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 dmax125.7
Rg (real space) rg_real34.03
Rg uncertainty (real space) rg_real_error1.03
I(0) (real space) i0_real2.0100e+08
I(0) uncertainty (real space) i0_real_error2.9290e+06
Rg (reciprocal space) rg_reciprocal34.01
I(0) (reciprocal space) i0_reciprocal201000000.0000
Solution quality estimate total_estimate0.8228
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.4
Skewness Skewness skewness0.463
Kurtosis Kurtosis kurtosis0.053
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha33060000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.606; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.921; Smooth: 0.954

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)