3zry

Rotor architecture in the F(1)-c(10)-ring complex of the yeast F-ATP synthase

Method: X-RAY DIFFRACTION Dmax: 195.6 Å Quality: GOOD

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 36–545 Chain B; UniProt 36–545 Chain C; UniProt 36–545 Not recorded ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00830) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P38077) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (Q12165) ATP SYNTHASE CATALYTIC SECTOR F1 EPSILON SUBUNIT × 1 (E9P9X4) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;10% PEG 4000, 100 MM SODIUM CHLORIDE, 100 MM HEPES PH 6.5 MIXED 1:1 WITH PROTEIN SOLUTION (10 MG/ML) CONTAINING 0.64 MM DDM, 25 MM TRIS PH 8.0, 100 MM SODIUM CHLORIDE, 25 MM TREHALOSE, 0.5 MM EDTA, 3 MM SODIUM AZIDE, 2 MM MAGNESIUM CHLORIDE, 0.04 MM ADP, 1 MM AMP-PNP, 0.1 MM DCCD, 2.5 MM DTT, 0.5 MM PMSF. Resolution 6.50 Å R-free 0.339

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
Chains and sequence ranges Author chain A; PDBConstruct 1–510; UniProt 36–545 Author chain B; PDBConstruct 1–510; UniProt 36–545 Author chain C; PDBConstruct 1–510; UniProt 36–545

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain D; UniProt 34–511 Chain E; UniProt 34–511 Chain F; UniProt 34–511 Not recorded ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P07251) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P38077) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (Q12165) ATP SYNTHASE CATALYTIC SECTOR F1 EPSILON SUBUNIT × 1 (E9P9X4) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;10% PEG 4000, 100 MM SODIUM CHLORIDE, 100 MM HEPES PH 6.5 MIXED 1:1 WITH PROTEIN SOLUTION (10 MG/ML) CONTAINING 0.64 MM DDM, 25 MM TRIS PH 8.0, 100 MM SODIUM CHLORIDE, 25 MM TREHALOSE, 0.5 MM EDTA, 3 MM SODIUM AZIDE, 2 MM MAGNESIUM CHLORIDE, 0.04 MM ADP, 1 MM AMP-PNP, 0.1 MM DCCD, 2.5 MM DTT, 0.5 MM PMSF. Resolution 6.50 Å R-free 0.339

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 2
Chains and sequence ranges Author chain D; PDBConstruct 1–478; UniProt 34–511 Author chain E; PDBConstruct 1–478; UniProt 34–511 Author chain F; PDBConstruct 1–478; UniProt 34–511

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain G; UniProt 34–311 Not recorded ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P07251) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00830) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (Q12165) ATP SYNTHASE CATALYTIC SECTOR F1 EPSILON SUBUNIT × 1 (E9P9X4) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;10% PEG 4000, 100 MM SODIUM CHLORIDE, 100 MM HEPES PH 6.5 MIXED 1:1 WITH PROTEIN SOLUTION (10 MG/ML) CONTAINING 0.64 MM DDM, 25 MM TRIS PH 8.0, 100 MM SODIUM CHLORIDE, 25 MM TREHALOSE, 0.5 MM EDTA, 3 MM SODIUM AZIDE, 2 MM MAGNESIUM CHLORIDE, 0.04 MM ADP, 1 MM AMP-PNP, 0.1 MM DCCD, 2.5 MM DTT, 0.5 MM PMSF. Resolution 6.50 Å R-free 0.339

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 3
Chains and sequence ranges 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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain H; UniProt 23–160 Not recorded ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P07251) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00830) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P38077) ATP SYNTHASE CATALYTIC SECTOR F1 EPSILON SUBUNIT × 1 (E9P9X4) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;10% PEG 4000, 100 MM SODIUM CHLORIDE, 100 MM HEPES PH 6.5 MIXED 1:1 WITH PROTEIN SOLUTION (10 MG/ML) CONTAINING 0.64 MM DDM, 25 MM TRIS PH 8.0, 100 MM SODIUM CHLORIDE, 25 MM TREHALOSE, 0.5 MM EDTA, 3 MM SODIUM AZIDE, 2 MM MAGNESIUM CHLORIDE, 0.04 MM ADP, 1 MM AMP-PNP, 0.1 MM DCCD, 2.5 MM DTT, 0.5 MM PMSF. Resolution 6.50 Å R-free 0.339

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 4
Chains and sequence ranges Author chain H; PDBConstruct 1–138; UniProt 23–160

ATP SYNTHASE CATALYTIC SECTOR F1 EPSILON SUBUNIT

OrganismNot specified

UniProt E9P9X4

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain I; UniProt 2–62 Not recorded ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 (P07251) ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 (P00830) ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 (P38077) ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 (Q12165) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;10% PEG 4000, 100 MM SODIUM CHLORIDE, 100 MM HEPES PH 6.5 MIXED 1:1 WITH PROTEIN SOLUTION (10 MG/ML) CONTAINING 0.64 MM DDM, 25 MM TRIS PH 8.0, 100 MM SODIUM CHLORIDE, 25 MM TREHALOSE, 0.5 MM EDTA, 3 MM SODIUM AZIDE, 2 MM MAGNESIUM CHLORIDE, 0.04 MM ADP, 1 MM AMP-PNP, 0.1 MM DCCD, 2.5 MM DTT, 0.5 MM PMSF. Resolution 6.50 Å R-free 0.339

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 E9P9X4_YEASX
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 1–61; UniProt 2–62

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
2 Protein homooligomer Homooligomer Protein × 10 PDB declaration: decameric(10) 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 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;10% PEG 4000, 100 MM SODIUM CHLORIDE, 100 MM HEPES PH 6.5 MIXED 1:1 WITH PROTEIN SOLUTION (10 MG/ML) CONTAINING 0.64 MM DDM, 25 MM TRIS PH 8.0, 100 MM SODIUM CHLORIDE, 25 MM TREHALOSE, 0.5 MM EDTA, 3 MM SODIUM AZIDE, 2 MM MAGNESIUM CHLORIDE, 0.04 MM ADP, 1 MM AMP-PNP, 0.1 MM DCCD, 2.5 MM DTT, 0.5 MM PMSF. Resolution 6.50 Å R-free 0.339

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 6
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

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 3zry

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3zry
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3zry
Deposition date deposition_date2011-06-21
Structure title titleRotor architecture in the F(1)-c(10)-ring complex of the yeast F-ATP synthase
Keywords keywordsHYDROLASE, ATP-BINDING, F(1)-F(O)ATP SYNTHASE, MITOCHONDRIA, MOLECULAR MOTOR, CENTRAL STALK, MEMBRANE PROTEIN, C-RING; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier56.74
Radius of gyration Rg (electron density) rg_electron58.82
Forward intensity I(0) i02450910000.00
Molecular weight molecular_weight427610.0 kDa
Excluded volume excluded_volume541200 ų
Envelope volume envelope_volume731960 ų
Hydration-shell volume shell_volume109590 ų
Envelope diameter envelope_diameter210.0
Shell Rg shell_rg57.64
Envelope Rg envelope_rg58.22
Shape Rg shape_rg58.74
Total Rg total_rg59.08
Total atoms total_atoms30100
Residues n_residues4032
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 dmax195.6
Rg (real space) rg_real57.34
Rg uncertainty (real space) rg_real_error2.24
I(0) (real space) i0_real2.4510e+09
I(0) uncertainty (real space) i0_real_error5.3490e+07
Rg (reciprocal space) rg_reciprocal56.23
I(0) (reciprocal space) i0_reciprocal2447000000.0000
Solution quality estimate total_estimate0.7706
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary55.9
Skewness Skewness skewness0.705
Kurtosis Kurtosis kurtosis0.003
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha459700000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.593; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.965; Smooth: 0.274

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (5)

9. Files and Curves (10)