6m0s

3.6A Yeast Vo state3 prime

Method: ELECTRON MICROSCOPY Dmax: 140.8 Å Quality: GOOD

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

V-type proton ATPase subunit a, vacuolar isoform

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P32563

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain A; UniProt 3–827 Not recorded V-type proton ATPase subunit e × 1 (Q3E7B6) Uncharacterized protein YPR170W-B × 1 (P0C5R9) V-type proton ATPase subunit d × 1 (P32366) ;V-type proton ATPase subunit c'' ; × 1 (P23968) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit c × 8 (P25515) V0 assembly protein 1 × 1 (P53262) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPH1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–825; UniProt 3–827

V-type proton ATPase subunit e

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt Q3E7B6

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain M; UniProt 1–71 Not recorded V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) Uncharacterized protein YPR170W-B × 1 (P0C5R9) V-type proton ATPase subunit d × 1 (P32366) ;V-type proton ATPase subunit c'' ; × 1 (P23968) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit c × 8 (P25515) V0 assembly protein 1 × 1 (P53262) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VA0E_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain M; PDBConstruct 1–71; UniProt 1–71

Uncharacterized protein YPR170W-B

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P0C5R9

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain O; UniProt 7–75 Not recorded V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit e × 1 (Q3E7B6) V-type proton ATPase subunit d × 1 (P32366) ;V-type proton ATPase subunit c'' ; × 1 (P23968) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit c × 8 (P25515) V0 assembly protein 1 × 1 (P53262) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

24 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name YP17B_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain O; PDBConstruct 1–69; UniProt 7–75

V-type proton ATPase subunit d

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P32366

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain B; UniProt 1–345 Not recorded V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit e × 1 (Q3E7B6) Uncharacterized protein YPR170W-B × 1 (P0C5R9) ;V-type proton ATPase subunit c'' ; × 1 (P23968) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit c × 8 (P25515) V0 assembly protein 1 × 1 (P53262) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

32 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VA0D_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 1–345; UniProt 1–345

;V-type proton ATPase subunit c'' ;

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P23968

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain C; UniProt 16–213 Not recorded V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit e × 1 (Q3E7B6) Uncharacterized protein YPR170W-B × 1 (P0C5R9) V-type proton ATPase subunit d × 1 (P32366) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit c × 8 (P25515) V0 assembly protein 1 × 1 (P53262) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATO_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain C; PDBConstruct 1–198; UniProt 16–213

;V-type proton ATPase subunit c' ;

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P32842

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain D; UniProt 7–164 Not recorded V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit e × 1 (Q3E7B6) Uncharacterized protein YPR170W-B × 1 (P0C5R9) V-type proton ATPase subunit d × 1 (P32366) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V-type proton ATPase subunit c × 8 (P25515) V0 assembly protein 1 × 1 (P53262) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATL2_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain D; PDBConstruct 1–158; UniProt 7–164

V-type proton ATPase subunit c

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P25515

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain E; UniProt 1–159 Chain F; UniProt 1–159 Chain G; UniProt 1–159 Chain H; UniProt 1–159 Chain I; UniProt 1–159 Chain J; UniProt 1–159 Chain K; UniProt 1–159 Chain L; UniProt 1–159 Not recorded V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit e × 1 (Q3E7B6) Uncharacterized protein YPR170W-B × 1 (P0C5R9) V-type proton ATPase subunit d × 1 (P32366) ;V-type proton ATPase subunit c'' ; × 1 (P23968) ;V-type proton ATPase subunit c' ; × 1 (P32842) V0 assembly protein 1 × 1 (P53262) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

32 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATL1_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain E; PDBConstruct 1–159; UniProt 1–159 Author chain F; PDBConstruct 1–159; UniProt 1–159 Author chain G; PDBConstruct 1–159; UniProt 1–159 Author chain H; PDBConstruct 1–159; UniProt 1–159 Author chain I; PDBConstruct 1–159; UniProt 1–159 Author chain J; PDBConstruct 1–159; UniProt 1–159 Author chain K; PDBConstruct 1–159; UniProt 1–159 Author chain L; PDBConstruct 1–159; UniProt 1–159

V0 assembly protein 1

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P53262

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain N; UniProt 212–263 Not recorded V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V-type proton ATPase subunit e × 1 (Q3E7B6) Uncharacterized protein YPR170W-B × 1 (P0C5R9) V-type proton ATPase subunit d × 1 (P32366) ;V-type proton ATPase subunit c'' ; × 1 (P23968) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit c × 8 (P25515) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

25 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VOA1_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain N; PDBConstruct 1–52; UniProt 212–263

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 6m0s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6m0s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6m0s
Deposition date deposition_date2020-02-22
Structure title title3.6A Yeast Vo state3 prime
Keywords keywordsV-ATPase, Vo sub-complex, rotary motor, transport protein; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.39
Radius of gyration Rg (electron density) rg_electron44.47
Forward intensity I(0) i01208690000.00
Molecular weight molecular_weight313000.0 kDa
Excluded volume excluded_volume402000 ų
Envelope volume envelope_volume579600 ų
Hydration-shell volume shell_volume102920 ų
Envelope diameter envelope_diameter145.6
Shell Rg shell_rg53.84
Envelope Rg envelope_rg43.31
Shape Rg shape_rg44.49
Total Rg total_rg44.85
Total atoms total_atoms44660
Residues n_residues2909
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 dmax140.8
Rg (real space) rg_real45.05
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real1.2090e+09
I(0) uncertainty (real space) i0_real_error2.0490e+07
Rg (reciprocal space) rg_reciprocal45.39
I(0) (reciprocal space) i0_reciprocal1209000000.0000
Solution quality estimate total_estimate0.8879
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary60.3
Skewness Skewness skewness0.078
Kurtosis Kurtosis kurtosis-0.469
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha119400000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.885; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.962; Smooth: 0.921

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)