1qo1

Molecular Architecture of the Rotary Motor in ATP Synthase from Yeast Mitochondria

Method: X-RAY DIFFRACTION Dmax: 192.2 Å Quality: REASONABLE

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

ATP SYNTHASE ALPHA CHAIN

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain A; UniProt 67–553 Chain B; UniProt 67–553 Chain C; UniProt 62–553 Not recorded ATP SYNTHASE BETA CHAIN × 3 (P00829) ATP SYNTHASE GAMMA CHAIN × 1 (P05631) ATP SYNTHASE DELTA CHAIN × 1 (P00832) ATP SYNTHASE PROTEIN 9 × 10 (P00844) X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 8;0.1 M TRIS/CL PH8.0, 12% PEG 6000, 150 MM NACL, 1 MM AMP-PNP, 40 MICROM ADP, 1 MM DTT, 0.02% NAN3, MIXED 1:1 WITH PROTEIN SOLUTION UNDER PARAFFIN OIL IN MICROBATCH PLATE., pH 8.00 Resolution 3.90 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 ATP0_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 24–510; UniProt 67–553 Author chain B; PDBConstruct 24–510; UniProt 67–553 Author chain C; PDBConstruct 19–510; UniProt 62–553

ATP SYNTHASE BETA CHAIN

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain D; UniProt 59–525 Chain E; UniProt 59–524 Chain F; UniProt 59–524 Not recorded ATP SYNTHASE ALPHA CHAIN × 3 (P19483) ATP SYNTHASE GAMMA CHAIN × 1 (P05631) ATP SYNTHASE DELTA CHAIN × 1 (P00832) ATP SYNTHASE PROTEIN 9 × 10 (P00844) X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 8;0.1 M TRIS/CL PH8.0, 12% PEG 6000, 150 MM NACL, 1 MM AMP-PNP, 40 MICROM ADP, 1 MM DTT, 0.02% NAN3, MIXED 1:1 WITH PROTEIN SOLUTION UNDER PARAFFIN OIL IN MICROBATCH PLATE., pH 8.00 Resolution 3.90 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 13–479; UniProt 59–525 Author chain E; PDBConstruct 13–478; UniProt 59–524 Author chain F; PDBConstruct 13–478; UniProt 59–524

ATP SYNTHASE GAMMA CHAIN

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain G; UniProt 26–69 Chain G; UniProt 102–115 Chain G; UniProt 234–297 Not recorded ATP SYNTHASE ALPHA CHAIN × 3 (P19483) ATP SYNTHASE BETA CHAIN × 3 (P00829) ATP SYNTHASE DELTA CHAIN × 1 (P00832) ATP SYNTHASE PROTEIN 9 × 10 (P00844) X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 8;0.1 M TRIS/CL PH8.0, 12% PEG 6000, 150 MM NACL, 1 MM AMP-PNP, 40 MICROM ADP, 1 MM DTT, 0.02% NAN3, MIXED 1:1 WITH PROTEIN SOLUTION UNDER PARAFFIN OIL IN MICROBATCH PLATE., pH 8.00 Resolution 3.90 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 1–44; UniProt 26–69 Author chain G; PDBConstruct 77–90; UniProt 102–115 Author chain G; PDBConstruct 209–272; UniProt 234–297

ATP SYNTHASE DELTA CHAIN

OrganismNot specified

UniProt P00832

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain J; UniProt 2–136 Not recorded ATP SYNTHASE ALPHA CHAIN × 3 (P19483) ATP SYNTHASE BETA CHAIN × 3 (P00829) ATP SYNTHASE GAMMA CHAIN × 1 (P05631) ATP SYNTHASE PROTEIN 9 × 10 (P00844) X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 8;0.1 M TRIS/CL PH8.0, 12% PEG 6000, 150 MM NACL, 1 MM AMP-PNP, 40 MICROM ADP, 1 MM DTT, 0.02% NAN3, MIXED 1:1 WITH PROTEIN SOLUTION UNDER PARAFFIN OIL IN MICROBATCH PLATE., pH 8.00 Resolution 3.90 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 ATPE_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain J; PDBConstruct 2–136; UniProt 2–136

ATP SYNTHASE PROTEIN 9

OrganismNot specified

UniProt P00844

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain K; UniProt 1–79 Chain L; UniProt 1–79 Chain M; UniProt 1–79 Chain N; UniProt 1–79 Chain O; UniProt 1–79 Chain P; UniProt 1–79 Chain Q; UniProt 1–79 Chain R; UniProt 1–79 Chain S; UniProt 1–79 Chain T; UniProt 1–79 Not recorded ATP SYNTHASE ALPHA CHAIN × 3 (P19483) ATP SYNTHASE BETA CHAIN × 3 (P00829) ATP SYNTHASE GAMMA CHAIN × 1 (P05631) ATP SYNTHASE DELTA CHAIN × 1 (P00832) X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 8;0.1 M TRIS/CL PH8.0, 12% PEG 6000, 150 MM NACL, 1 MM AMP-PNP, 40 MICROM ADP, 1 MM DTT, 0.02% NAN3, MIXED 1:1 WITH PROTEIN SOLUTION UNDER PARAFFIN OIL IN MICROBATCH PLATE., pH 8.00 Resolution 3.90 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 ATPL_ECOLI
Isoform
PDB entities 5
Chains and sequence ranges Author chain K; PDBConstruct 1–79; UniProt 1–79 Author chain L; PDBConstruct 1–79; UniProt 1–79 Author chain M; PDBConstruct 1–79; UniProt 1–79 Author chain N; PDBConstruct 1–79; UniProt 1–79 Author chain O; PDBConstruct 1–79; UniProt 1–79 Author chain P; PDBConstruct 1–79; UniProt 1–79 Author chain Q; PDBConstruct 1–79; UniProt 1–79 Author chain R; PDBConstruct 1–79; UniProt 1–79 Author chain S; PDBConstruct 1–79; UniProt 1–79 Author chain T; PDBConstruct 1–79; UniProt 1–79

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 1qo1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1qo1
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1qo1
Deposition date deposition_date1999-11-01
Structure title titleMolecular Architecture of the Rotary Motor in ATP Synthase from Yeast Mitochondria
Keywords keywordsATP SYNTHASE, LOW RESOLUTION MODEL, C-ALPHA ONLY; ATP SYNTHASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier59.22
Radius of gyration Rg (electron density) rg_electron60.82
Forward intensity I(0) i02349110000.00
Molecular weight molecular_weight420450.0 kDa
Excluded volume excluded_volume522900 ų
Envelope volume envelope_volume527670 ų
Hydration-shell volume shell_volume83436 ų
Envelope diameter envelope_diameter212.1
Shell Rg shell_rg54.11
Envelope Rg envelope_rg55.67
Shape Rg shape_rg61.08
Total Rg total_rg60.67
Total atoms total_atoms
Residues n_residues
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 dmax192.2
Rg (real space) rg_real60.02
Rg uncertainty (real space) rg_real_error1.86
I(0) (real space) i0_real2.3490e+09
I(0) uncertainty (real space) i0_real_error4.8540e+07
Rg (reciprocal space) rg_reciprocal58.51
I(0) (reciprocal space) i0_reciprocal2343000000.0000
Solution quality estimate total_estimate0.5192
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary56.9
Skewness Skewness skewness0.663
Kurtosis Kurtosis kurtosis-0.307
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha252100000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.597; Stabil: 1.000; Sysdev: 0.009; Positv: 1.000; Valcen: 0.902; Smooth: 0.027

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 18 domains

SCOP 2.08 (18 domains)

Domain ID domain_idd1qo1a_
Class classi — Low resolution protein structures
Fold Fold foldi.3 — ATP synthase
Superfamily Superfamily superfamilyi.3.1 — ATP synthase
Family Family familyi.3.1.1 — ATP synthase
Domain ID domain_idd1qo1b_
Class classi — Low resolution protein structures
Fold Fold foldi.3 — ATP synthase
Superfamily Superfamily superfamilyi.3.1 — ATP synthase
Family Family familyi.3.1.1 — ATP synthase
Domain ID domain_idd1qo1c_
Class classi — Low resolution protein structures
Fold Fold foldi.3 — ATP synthase
Superfamily Superfamily superfamilyi.3.1 — ATP synthase
Family Family familyi.3.1.1 — ATP synthase
Domain ID domain_idd1qo1d_
Class classi — Low resolution protein structures
Fold Fold foldi.3 — ATP synthase
Superfamily Superfamily superfamilyi.3.1 — ATP synthase
Family Family familyi.3.1.1 — ATP synthase
Domain ID domain_idd1qo1e_
Class classi — Low resolution protein structures
Fold Fold foldi.3 — ATP synthase
Superfamily Superfamily superfamilyi.3.1 — ATP synthase
Family Family familyi.3.1.1 — ATP synthase
Domain ID domain_idd1qo1f_
Class classi — Low resolution protein structures
Fold Fold foldi.3 — ATP synthase
Superfamily Superfamily superfamilyi.3.1 — ATP synthase
Family Family familyi.3.1.1 — ATP synthase
Domain ID domain_idd1qo1g_
Class classi — Low resolution protein structures
Fold Fold foldi.3 — ATP synthase
Superfamily Superfamily superfamilyi.3.1 — ATP synthase
Family Family familyi.3.1.1 — ATP synthase
Domain ID domain_idd1qo1j_
Class classi — Low resolution protein structures
Fold Fold foldi.3 — ATP synthase
Superfamily Superfamily superfamilyi.3.1 — ATP synthase
Family Family familyi.3.1.1 — ATP synthase
Domain ID domain_idd1qo1k_
Class classi — Low resolution protein structures
Fold Fold foldi.3 — ATP synthase
Superfamily Superfamily superfamilyi.3.1 — ATP synthase
Family Family familyi.3.1.1 — ATP synthase
Domain ID domain_idd1qo1l_
Class classi — Low resolution protein structures
Fold Fold foldi.3 — ATP synthase
Superfamily Superfamily superfamilyi.3.1 — ATP synthase
Family Family familyi.3.1.1 — ATP synthase
Domain ID domain_idd1qo1m_
Class classi — Low resolution protein structures
Fold Fold foldi.3 — ATP synthase
Superfamily Superfamily superfamilyi.3.1 — ATP synthase
Family Family familyi.3.1.1 — ATP synthase
Domain ID domain_idd1qo1n_
Class classi — Low resolution protein structures
Fold Fold foldi.3 — ATP synthase
Superfamily Superfamily superfamilyi.3.1 — ATP synthase
Family Family familyi.3.1.1 — ATP synthase
Domain ID domain_idd1qo1o_
Class classi — Low resolution protein structures
Fold Fold foldi.3 — ATP synthase
Superfamily Superfamily superfamilyi.3.1 — ATP synthase
Family Family familyi.3.1.1 — ATP synthase
Domain ID domain_idd1qo1p_
Class classi — Low resolution protein structures
Fold Fold foldi.3 — ATP synthase
Superfamily Superfamily superfamilyi.3.1 — ATP synthase
Family Family familyi.3.1.1 — ATP synthase
Domain ID domain_idd1qo1q_
Class classi — Low resolution protein structures
Fold Fold foldi.3 — ATP synthase
Superfamily Superfamily superfamilyi.3.1 — ATP synthase
Family Family familyi.3.1.1 — ATP synthase
Domain ID domain_idd1qo1r_
Class classi — Low resolution protein structures
Fold Fold foldi.3 — ATP synthase
Superfamily Superfamily superfamilyi.3.1 — ATP synthase
Family Family familyi.3.1.1 — ATP synthase
Domain ID domain_idd1qo1s_
Class classi — Low resolution protein structures
Fold Fold foldi.3 — ATP synthase
Superfamily Superfamily superfamilyi.3.1 — ATP synthase
Family Family familyi.3.1.1 — ATP synthase
Domain ID domain_idd1qo1t_
Class classi — Low resolution protein structures
Fold Fold foldi.3 — ATP synthase
Superfamily Superfamily superfamilyi.3.1 — ATP synthase
Family Family familyi.3.1.1 — ATP synthase

8. Citations (4)

9. Files and Curves (10)