6vqi

Mammalian V-ATPase from rat brain collar and peripheral stalks rotational state 1 (from focused refinement)

Method: ELECTRON MICROSCOPY Dmax: 173.0 Å Quality: REASONABLE

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

V-type proton ATPase subunit C 1

OrganismNot specified

UniProt Q5FVI6

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain G; UniProt 1–382 Not recorded V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit G × 3 (Q8R2H0) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 4.30 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 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATC1_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain G; PDBConstruct 1–382; UniProt 1–382

V-type proton ATPase subunit E 1

OrganismNot specified

UniProt Q6PCU2

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain I; UniProt 1–226 Chain J; UniProt 1–226 Chain K; UniProt 1–226 Not recorded V-type proton ATPase subunit C 1 × 1 (Q5FVI6) V-type proton ATPase subunit G × 3 (Q8R2H0) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 4.30 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 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATE1_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; PDBConstruct 1–226; UniProt 1–226 Author chain J; PDBConstruct 1–226; UniProt 1–226 Author chain K; PDBConstruct 1–226; UniProt 1–226

V-type proton ATPase subunit G

OrganismNot specified

UniProt Q8R2H0

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain M; UniProt 1–118 Chain N; UniProt 1–118 Chain O; UniProt 1–118 Not recorded V-type proton ATPase subunit C 1 × 1 (Q5FVI6) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 4.30 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 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8R2H0_RAT
Isoform
PDB entities 3
Chains and sequence ranges Author chain M; PDBConstruct 1–118; UniProt 1–118 Author chain N; PDBConstruct 1–118; UniProt 1–118 Author chain O; PDBConstruct 1–118; UniProt 1–118

V-type proton ATPase 116 kDa subunit a isoform 1

OrganismNot specified

UniProt P25286

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain a; UniProt 1–838 Not recorded V-type proton ATPase subunit C 1 × 1 (Q5FVI6) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit G × 3 (Q8R2H0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 4.30 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 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPP1_RAT
Isoform
PDB entities 4
Chains and sequence ranges Author chain a; PDBConstruct 1–838; UniProt 1–838

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 6vqi

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6vqi
Deposition date deposition_date2020-02-05
Structure title titleMammalian V-ATPase from rat brain collar and peripheral stalks rotational state 1 (from focused refinement)
Keywords keywordsmembrane protein complex, rotary atpase, PROTON TRANSPORT; PROTON TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier62.38
Radius of gyration Rg (electron density) rg_electron62.20
Forward intensity I(0) i0116502000.00
Molecular weight molecular_weight73917.0 kDa
Excluded volume excluded_volume85569 ų
Envelope volume envelope_volume263440 ų
Hydration-shell volume shell_volume37948 ų
Envelope diameter envelope_diameter168.6
Shell Rg shell_rg62.47
Envelope Rg envelope_rg55.56
Shape Rg shape_rg62.18
Total Rg total_rg62.28
Total atoms total_atoms5278
Residues n_residues1062
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 dmax173.0
Rg (real space) rg_real62.11
Rg uncertainty (real space) rg_real_error1.16
I(0) (real space) i0_real1.1650e+08
I(0) uncertainty (real space) i0_real_error2.3660e+06
Rg (reciprocal space) rg_reciprocal62.52
I(0) (reciprocal space) i0_reciprocal116600000.0000
Solution quality estimate total_estimate0.6683
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary110.7
Skewness Skewness skewness-0.262
Kurtosis Kurtosis kurtosis-1.087
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5244000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.311; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.752; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)