7une

The V1 region of bovine V-ATPase in complex with human mEAK7 (focused refinement)

Method: ELECTRON MICROSCOPY Dmax: 185.8 Å Quality: GOOD

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

V-type proton ATPase catalytic subunit A

OrganismNot specified

UniProt P31404

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: tetradecameric(14) Consistent with protein copy count Chain L; UniProt 1–617 Chain M; UniProt 1–617 Chain N; UniProt 1–617 Not recorded V-type proton ATPase subunit D × 1 (A0A3Q1M4W9) KIAA1609 protein, isoform CRA_a × 1 (D3DUL8) V-type proton ATPase subunit E 1 × 3 (P11019) V-type proton ATPase subunit B, brain isoform × 3 (P31408) V-type proton ATPase subunit G × 3 (Q0VCV6) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.73 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATA_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain L; PDBConstruct 1–617; UniProt 1–617 Author chain M; PDBConstruct 1–617; UniProt 1–617 Author chain N; PDBConstruct 1–617; UniProt 1–617

V-type proton ATPase subunit D

OrganismNot specified

UniProt A0A3Q1M4W9

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: tetradecameric(14) Consistent with protein copy count Chain D; UniProt 1–247 Not recorded V-type proton ATPase catalytic subunit A × 3 (P31404) KIAA1609 protein, isoform CRA_a × 1 (D3DUL8) V-type proton ATPase subunit E 1 × 3 (P11019) V-type proton ATPase subunit B, brain isoform × 3 (P31408) V-type proton ATPase subunit G × 3 (Q0VCV6) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.73 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A3Q1M4W9_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–247; UniProt 1–247

KIAA1609 protein, isoform CRA_a

Homo sapiens

UniProt D3DUL8

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: tetradecameric(14) Consistent with protein copy count Chain U; UniProt 2–456 Not recorded V-type proton ATPase catalytic subunit A × 3 (P31404) V-type proton ATPase subunit D × 1 (A0A3Q1M4W9) V-type proton ATPase subunit E 1 × 3 (P11019) V-type proton ATPase subunit B, brain isoform × 3 (P31408) V-type proton ATPase subunit G × 3 (Q0VCV6) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.73 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name D3DUL8_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain U; PDBConstruct 9–463; UniProt 2–456

V-type proton ATPase subunit E 1

OrganismNot specified

UniProt P11019

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: tetradecameric(14) Consistent with protein copy count Chain b; UniProt 1–226 Chain c; UniProt 1–226 Chain d; UniProt 1–226 Not recorded V-type proton ATPase catalytic subunit A × 3 (P31404) V-type proton ATPase subunit D × 1 (A0A3Q1M4W9) KIAA1609 protein, isoform CRA_a × 1 (D3DUL8) V-type proton ATPase subunit B, brain isoform × 3 (P31408) V-type proton ATPase subunit G × 3 (Q0VCV6) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.73 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATE1_BOVIN
Isoform
PDB entities 4
Chains and sequence ranges Author chain b; PDBConstruct 1–226; UniProt 1–226 Author chain c; PDBConstruct 1–226; UniProt 1–226 Author chain d; PDBConstruct 1–226; UniProt 1–226

V-type proton ATPase subunit B, brain isoform

OrganismNot specified

UniProt P31408

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: tetradecameric(14) Consistent with protein copy count Chain O; UniProt 1–511 Chain P; UniProt 1–511 Chain Q; UniProt 1–511 Not recorded V-type proton ATPase catalytic subunit A × 3 (P31404) V-type proton ATPase subunit D × 1 (A0A3Q1M4W9) KIAA1609 protein, isoform CRA_a × 1 (D3DUL8) V-type proton ATPase subunit E 1 × 3 (P11019) V-type proton ATPase subunit G × 3 (Q0VCV6) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.73 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATB2_BOVIN
Isoform
PDB entities 5
Chains and sequence ranges Author chain O; PDBConstruct 1–511; UniProt 1–511 Author chain P; PDBConstruct 1–511; UniProt 1–511 Author chain Q; PDBConstruct 1–511; UniProt 1–511

V-type proton ATPase subunit G

OrganismNot specified

UniProt Q0VCV6

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: tetradecameric(14) Consistent with protein copy count Chain e; UniProt 1–118 Chain f; UniProt 1–118 Chain g; UniProt 1–118 Not recorded V-type proton ATPase catalytic subunit A × 3 (P31404) V-type proton ATPase subunit D × 1 (A0A3Q1M4W9) KIAA1609 protein, isoform CRA_a × 1 (D3DUL8) V-type proton ATPase subunit E 1 × 3 (P11019) V-type proton ATPase subunit B, brain isoform × 3 (P31408) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.73 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q0VCV6_BOVIN
Isoform
PDB entities 6
Chains and sequence ranges Author chain e; PDBConstruct 1–118; UniProt 1–118 Author chain f; PDBConstruct 1–118; UniProt 1–118 Author chain g; 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 7une

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7une
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7une
Deposition date deposition_date2022-04-10
Structure title titleThe V1 region of bovine V-ATPase in complex with human mEAK7 (focused refinement)
Keywords keywordsproton transport, mTOR signaling; PROTON TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier54.68
Radius of gyration Rg (electron density) rg_electron54.15
Forward intensity I(0) i03769140000.00
Molecular weight molecular_weight515390.0 kDa
Excluded volume excluded_volume645420 ų
Envelope volume envelope_volume931410 ų
Hydration-shell volume shell_volume136890 ų
Envelope diameter envelope_diameter202.2
Shell Rg shell_rg61.51
Envelope Rg envelope_rg54.53
Shape Rg shape_rg54.15
Total Rg total_rg54.36
Total atoms total_atoms36209
Residues n_residues4663
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 dmax185.8
Rg (real space) rg_real54.59
Rg uncertainty (real space) rg_real_error1.69
I(0) (real space) i0_real3.7690e+09
I(0) uncertainty (real space) i0_real_error7.6450e+07
Rg (reciprocal space) rg_reciprocal54.74
I(0) (reciprocal space) i0_reciprocal3770000000.0000
Solution quality estimate total_estimate0.8490
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary64.1
Skewness Skewness skewness0.388
Kurtosis Kurtosis kurtosis-0.005
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha677400000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.750; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.969; Smooth: 0.815

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)