5d80

Crystal Structure of Yeast V1-ATPase in the Autoinhibited Form

Method: X-RAY DIFFRACTION Dmax: 287.7 Å Quality: GOOD

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

V-type proton ATPase catalytic subunit A

OrganismNot specified

UniProt P17255

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 1–283 Chain A; UniProt 738–1071 Chain B; UniProt 1–283 Chain B; UniProt 738–1071 Chain C; UniProt 1–283 Chain C; UniProt 738–1071 Not recorded V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;8.25% PEG 8000, 0.25 M Ammonium Sulfate, 0.1 M HEPES pH 7.5, 0.05 M Strontium Chloride Resolution 6.20 Å R-free 0.302
2 Protein heterocomplex Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain a; UniProt 1–283 Chain a; UniProt 738–1071 Chain b; UniProt 1–283 Chain b; UniProt 738–1071 Chain c; UniProt 1–283 Chain c; UniProt 738–1071 Not recorded V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;8.25% PEG 8000, 0.25 M Ammonium Sulfate, 0.1 M HEPES pH 7.5, 0.05 M Strontium Chloride Resolution 6.20 Å R-free 0.302

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.

15 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATA_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–283; UniProt 1–283 Author chain A; PDBConstruct 284–617; UniProt 738–1071 Author chain B; PDBConstruct 1–283; UniProt 1–283 Author chain B; PDBConstruct 284–617; UniProt 738–1071 Author chain C; PDBConstruct 1–283; UniProt 1–283 Author chain C; PDBConstruct 284–617; UniProt 738–1071 Author chain a; PDBConstruct 1–283; UniProt 1–283 Author chain a; PDBConstruct 284–617; UniProt 738–1071 Author chain b; PDBConstruct 1–283; UniProt 1–283 Author chain b; PDBConstruct 284–617; UniProt 738–1071 Author chain c; PDBConstruct 1–283; UniProt 1–283 Author chain c; PDBConstruct 284–617; UniProt 738–1071

V-type proton ATPase subunit B

OrganismNot specified

UniProt P16140

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 1–517 Chain E; UniProt 1–517 Chain F; UniProt 1–517 Not recorded V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;8.25% PEG 8000, 0.25 M Ammonium Sulfate, 0.1 M HEPES pH 7.5, 0.05 M Strontium Chloride Resolution 6.20 Å R-free 0.302
2 Protein heterocomplex Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain d; UniProt 1–517 Chain e; UniProt 1–517 Chain f; UniProt 1–517 Not recorded V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;8.25% PEG 8000, 0.25 M Ammonium Sulfate, 0.1 M HEPES pH 7.5, 0.05 M Strontium Chloride Resolution 6.20 Å R-free 0.302

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.

18 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATB_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–517; UniProt 1–517 Author chain E; PDBConstruct 1–517; UniProt 1–517 Author chain F; PDBConstruct 1–517; UniProt 1–517 Author chain d; PDBConstruct 1–517; UniProt 1–517 Author chain e; PDBConstruct 1–517; UniProt 1–517 Author chain f; PDBConstruct 1–517; UniProt 1–517

V-type proton ATPase subunit H

OrganismNot specified

UniProt P41807

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 H; UniProt 1–478 Not recorded V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;8.25% PEG 8000, 0.25 M Ammonium Sulfate, 0.1 M HEPES pH 7.5, 0.05 M Strontium Chloride Resolution 6.20 Å R-free 0.302
2 Protein heterocomplex Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain h; UniProt 1–478 Not recorded V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;8.25% PEG 8000, 0.25 M Ammonium Sulfate, 0.1 M HEPES pH 7.5, 0.05 M Strontium Chloride Resolution 6.20 Å R-free 0.302

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 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATH_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain H; PDBConstruct 1–478; UniProt 1–478 Author chain h; PDBConstruct 1–478; UniProt 1–478

V-type proton ATPase subunit G

OrganismNot specified

UniProt P48836

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 J; UniProt 2–114 Chain L; UniProt 2–114 Chain N; UniProt 2–114 Not recorded V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;8.25% PEG 8000, 0.25 M Ammonium Sulfate, 0.1 M HEPES pH 7.5, 0.05 M Strontium Chloride Resolution 6.20 Å R-free 0.302
2 Protein heterocomplex Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain j; UniProt 2–114 Chain l; UniProt 2–114 Chain n; UniProt 2–114 Not recorded V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;8.25% PEG 8000, 0.25 M Ammonium Sulfate, 0.1 M HEPES pH 7.5, 0.05 M Strontium Chloride Resolution 6.20 Å R-free 0.302

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.

20 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATG_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain J; PDBConstruct 10–122; UniProt 2–114 Author chain L; PDBConstruct 10–122; UniProt 2–114 Author chain N; PDBConstruct 10–122; UniProt 2–114 Author chain j; PDBConstruct 10–122; UniProt 2–114 Author chain l; PDBConstruct 10–122; UniProt 2–114 Author chain n; PDBConstruct 10–122; UniProt 2–114

V-type proton ATPase subunit E

OrganismNot specified

UniProt P22203

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 I; UniProt 1–233 Chain K; UniProt 1–233 Chain M; UniProt 1–233 Not recorded V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;8.25% PEG 8000, 0.25 M Ammonium Sulfate, 0.1 M HEPES pH 7.5, 0.05 M Strontium Chloride Resolution 6.20 Å R-free 0.302
2 Protein heterocomplex Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain i; UniProt 1–233 Chain k; UniProt 1–233 Chain m; UniProt 1–233 Not recorded V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;8.25% PEG 8000, 0.25 M Ammonium Sulfate, 0.1 M HEPES pH 7.5, 0.05 M Strontium Chloride Resolution 6.20 Å R-free 0.302

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.

21 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATE_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 1–233; UniProt 1–233 Author chain K; PDBConstruct 1–233; UniProt 1–233 Author chain M; PDBConstruct 1–233; UniProt 1–233 Author chain i; PDBConstruct 1–233; UniProt 1–233 Author chain k; PDBConstruct 1–233; UniProt 1–233 Author chain m; PDBConstruct 1–233; UniProt 1–233

V-type proton ATPase subunit D

OrganismNot specified

UniProt P32610

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 G; UniProt 1–256 Not recorded V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit F × 1 (P39111) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;8.25% PEG 8000, 0.25 M Ammonium Sulfate, 0.1 M HEPES pH 7.5, 0.05 M Strontium Chloride Resolution 6.20 Å R-free 0.302
2 Protein heterocomplex Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain g; UniProt 1–256 Not recorded V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit F × 1 (P39111) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;8.25% PEG 8000, 0.25 M Ammonium Sulfate, 0.1 M HEPES pH 7.5, 0.05 M Strontium Chloride Resolution 6.20 Å R-free 0.302

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.

19 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATD_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain G; PDBConstruct 1–256; UniProt 1–256 Author chain g; PDBConstruct 1–256; UniProt 1–256

V-type proton ATPase subunit F

OrganismNot specified

UniProt P39111

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 1–118 Not recorded V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit D × 1 (P32610) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;8.25% PEG 8000, 0.25 M Ammonium Sulfate, 0.1 M HEPES pH 7.5, 0.05 M Strontium Chloride Resolution 6.20 Å R-free 0.302
2 Protein heterocomplex Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain o; UniProt 1–118 Not recorded V-type proton ATPase catalytic subunit A × 3 (P17255) V-type proton ATPase subunit B × 3 (P16140) V-type proton ATPase subunit H × 1 (P41807) V-type proton ATPase subunit G × 3 (P48836) V-type proton ATPase subunit E × 3 (P22203) V-type proton ATPase subunit D × 1 (P32610) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;8.25% PEG 8000, 0.25 M Ammonium Sulfate, 0.1 M HEPES pH 7.5, 0.05 M Strontium Chloride Resolution 6.20 Å R-free 0.302

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.

19 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATF_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain O; PDBConstruct 1–118; UniProt 1–118 Author chain o; PDBConstruct 1–118; UniProt 1–118

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 5d80

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5d80
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5d80
Deposition date deposition_date2015-08-14
Structure title titleCrystal Structure of Yeast V1-ATPase in the Autoinhibited Form
Keywords keywordsHydrolase, Autoinhibition; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier81.24
Radius of gyration Rg (electron density) rg_electron81.42
Forward intensity I(0) i09193720000.00
Molecular weight molecular_weight662810.0 kDa
Excluded volume excluded_volume761770 ų
Envelope volume envelope_volume1896100 ų
Hydration-shell volume shell_volume193380 ų
Envelope diameter envelope_diameter289.4
Shell Rg shell_rg79.00
Envelope Rg envelope_rg77.99
Shape Rg shape_rg81.41
Total Rg total_rg81.42
Total atoms total_atoms47363
Residues n_residues9600
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 dmax287.7
Rg (real space) rg_real85.44
Rg uncertainty (real space) rg_real_error1.82
I(0) (real space) i0_real9.2300e+09
I(0) uncertainty (real space) i0_real_error1.9680e+08
Rg (reciprocal space) rg_reciprocal80.77
I(0) (reciprocal space) i0_reciprocal9181000000.0000
Solution quality estimate total_estimate0.8760
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary75.7
Skewness Skewness skewness0.476
Kurtosis Kurtosis kurtosis-0.240
Angular range angular_range— – 0.0950 −1
Current regularization parameter α current_alpha1.2170
Highest regularization parameter α highest_alpha3167000000.0000
Real-space data points n_real_points20
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.835; Stabil: 0.863; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.324

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)