9cop

Yeast RAVE bound to V-ATPase V1 complex

Method: ELECTRON MICROSCOPY Dmax: 224.6 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 × 14 PDB declaration: 14-meric(14) Consistent with protein copy count Chain A; UniProt 1–1071 Chain E; UniProt 1–1071 Not recorded V-type proton ATPase subunit B × 2 (P16140) V-type proton ATPase subunit E × 2 (P22203) V-type proton ATPase subunit G × 2 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit H × 1 (P41807) Regulator of V-ATPase in vacuolar membrane protein 1 × 1 (P47104) Regulator of V-ATPase in vacuolar membrane protein 2 × 1 (Q03956) Suppressor of kinetochore protein 1 × 1 (P52286) MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

15 other PDB entries and 19 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 1–1071; UniProt 1–1071 Author chain E; PDBConstruct 1–1071; UniProt 1–1071

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 × 14 PDB declaration: 14-meric(14) Consistent with protein copy count Chain B; UniProt 1–517 Chain F; UniProt 1–517 Not recorded V-type proton ATPase catalytic subunit A × 2 (P17255) V-type proton ATPase subunit E × 2 (P22203) V-type proton ATPase subunit G × 2 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit H × 1 (P41807) Regulator of V-ATPase in vacuolar membrane protein 1 × 1 (P47104) Regulator of V-ATPase in vacuolar membrane protein 2 × 1 (Q03956) Suppressor of kinetochore protein 1 × 1 (P52286) MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

18 other PDB entries and 20 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 B; PDBConstruct 1–517; UniProt 1–517 Author chain F; PDBConstruct 1–517; UniProt 1–517

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 × 14 PDB declaration: 14-meric(14) Consistent with protein copy count Chain I; UniProt 1–233 Chain K; UniProt 1–233 Not recorded V-type proton ATPase catalytic subunit A × 2 (P17255) V-type proton ATPase subunit B × 2 (P16140) V-type proton ATPase subunit G × 2 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit H × 1 (P41807) Regulator of V-ATPase in vacuolar membrane protein 1 × 1 (P47104) Regulator of V-ATPase in vacuolar membrane protein 2 × 1 (Q03956) Suppressor of kinetochore protein 1 × 1 (P52286) MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

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

View Construct and Data Evidence
UniProt name VATE_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain I; PDBConstruct 1–233; UniProt 1–233 Author chain K; PDBConstruct 1–233; UniProt 1–233

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 × 14 PDB declaration: 14-meric(14) Consistent with protein copy count Chain J; UniProt 1–114 Chain L; UniProt 1–114 Not recorded V-type proton ATPase catalytic subunit A × 2 (P17255) V-type proton ATPase subunit B × 2 (P16140) V-type proton ATPase subunit E × 2 (P22203) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit H × 1 (P41807) Regulator of V-ATPase in vacuolar membrane protein 1 × 1 (P47104) Regulator of V-ATPase in vacuolar membrane protein 2 × 1 (Q03956) Suppressor of kinetochore protein 1 × 1 (P52286) MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

20 other PDB entries and 23 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 1–114; UniProt 1–114 Author chain L; PDBConstruct 1–114; UniProt 1–114

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 × 14 PDB declaration: 14-meric(14) Consistent with protein copy count Chain M; UniProt 1–256 Not recorded V-type proton ATPase catalytic subunit A × 2 (P17255) V-type proton ATPase subunit B × 2 (P16140) V-type proton ATPase subunit E × 2 (P22203) V-type proton ATPase subunit G × 2 (P48836) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit H × 1 (P41807) Regulator of V-ATPase in vacuolar membrane protein 1 × 1 (P47104) Regulator of V-ATPase in vacuolar membrane protein 2 × 1 (Q03956) Suppressor of kinetochore protein 1 × 1 (P52286) MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

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

View Construct and Data Evidence
UniProt name VATD_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain M; 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 × 14 PDB declaration: 14-meric(14) Consistent with protein copy count Chain N; UniProt 2–118 Not recorded V-type proton ATPase catalytic subunit A × 2 (P17255) V-type proton ATPase subunit B × 2 (P16140) V-type proton ATPase subunit E × 2 (P22203) V-type proton ATPase subunit G × 2 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit H × 1 (P41807) Regulator of V-ATPase in vacuolar membrane protein 1 × 1 (P47104) Regulator of V-ATPase in vacuolar membrane protein 2 × 1 (Q03956) Suppressor of kinetochore protein 1 × 1 (P52286) MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

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

View Construct and Data Evidence
UniProt name VATF_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain N; PDBConstruct 1–117; UniProt 2–118

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 × 14 PDB declaration: 14-meric(14) Consistent with protein copy count Chain P; UniProt 1–478 Not recorded V-type proton ATPase catalytic subunit A × 2 (P17255) V-type proton ATPase subunit B × 2 (P16140) V-type proton ATPase subunit E × 2 (P22203) V-type proton ATPase subunit G × 2 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) Regulator of V-ATPase in vacuolar membrane protein 1 × 1 (P47104) Regulator of V-ATPase in vacuolar membrane protein 2 × 1 (Q03956) Suppressor of kinetochore protein 1 × 1 (P52286) MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATH_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain P; PDBConstruct 1–478; UniProt 1–478

Regulator of V-ATPase in vacuolar membrane protein 1

OrganismNot specified

UniProt P47104

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 × 14 PDB declaration: 14-meric(14) Consistent with protein copy count Chain x; UniProt 1–1357 Not recorded V-type proton ATPase catalytic subunit A × 2 (P17255) V-type proton ATPase subunit B × 2 (P16140) V-type proton ATPase subunit E × 2 (P22203) V-type proton ATPase subunit G × 2 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit H × 1 (P41807) Regulator of V-ATPase in vacuolar membrane protein 2 × 1 (Q03956) Suppressor of kinetochore protein 1 × 1 (P52286) MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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 RAV1_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain x; PDBConstruct 1–1357; UniProt 1–1357

Regulator of V-ATPase in vacuolar membrane protein 2

OrganismNot specified

UniProt Q03956

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 × 14 PDB declaration: 14-meric(14) Consistent with protein copy count Chain y; UniProt 1–351 Not recorded V-type proton ATPase catalytic subunit A × 2 (P17255) V-type proton ATPase subunit B × 2 (P16140) V-type proton ATPase subunit E × 2 (P22203) V-type proton ATPase subunit G × 2 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit H × 1 (P41807) Regulator of V-ATPase in vacuolar membrane protein 1 × 1 (P47104) Suppressor of kinetochore protein 1 × 1 (P52286) MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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 RAV2_YEAST
Isoform
PDB entities 9
Chains and sequence ranges Author chain y; PDBConstruct 1–351; UniProt 1–351

Suppressor of kinetochore protein 1

OrganismNot specified

UniProt P52286

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 × 14 PDB declaration: 14-meric(14) Consistent with protein copy count Chain z; UniProt 1–194 Not recorded V-type proton ATPase catalytic subunit A × 2 (P17255) V-type proton ATPase subunit B × 2 (P16140) V-type proton ATPase subunit E × 2 (P22203) V-type proton ATPase subunit G × 2 (P48836) V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit H × 1 (P41807) Regulator of V-ATPase in vacuolar membrane protein 1 × 1 (P47104) Regulator of V-ATPase in vacuolar membrane protein 2 × 1 (Q03956) MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

13 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SKP1_YEAST
Isoform
PDB entities 10
Chains and sequence ranges Author chain z; PDBConstruct 1–194; UniProt 1–194

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 9cop

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9cop
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9cop
Deposition date deposition_date2024-07-17
Structure title titleYeast RAVE bound to V-ATPase V1 complex
Keywords keywordsV-ATPase, RAVE, assembly, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier74.85
Radius of gyration Rg (electron density) rg_electron74.16
Forward intensity I(0) i03841770000.00
Molecular weight molecular_weight516930.0 kDa
Excluded volume excluded_volume643550 ų
Envelope volume envelope_volume1116200 ų
Hydration-shell volume shell_volume128010 ų
Envelope diameter envelope_diameter258.0
Shell Rg shell_rg67.78
Envelope Rg envelope_rg75.38
Shape Rg shape_rg74.35
Total Rg total_rg73.37
Total atoms total_atoms70017
Residues n_residues5041
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 dmax224.6
Rg (real space) rg_real74.84
Rg uncertainty (real space) rg_real_error1.48
I(0) (real space) i0_real3.8340e+09
I(0) uncertainty (real space) i0_real_error8.1710e+07
Rg (reciprocal space) rg_reciprocal73.44
I(0) (reciprocal space) i0_reciprocal3828000000.0000
Solution quality estimate total_estimate0.8352
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary64.2
Skewness Skewness skewness0.349
Kurtosis Kurtosis kurtosis-0.697
Angular range angular_range— – 0.1050 −1
Current regularization parameter α current_alpha0.0189
Highest regularization parameter α highest_alpha156200000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.956; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.001

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (1)

9. Files and Curves (10)