6vqc

Mammalian V-ATPase from rat brain membrane-embedded Vo region rotational state 1 (from focused refinement)

Method: ELECTRON MICROSCOPY Dmax: 143.1 Å Quality: GOOD

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

ATPase H+-transporting V1 subunit D

OrganismNot specified

UniProt Q6P503

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain H; UniProt 1–247 Not recorded V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit × 1 (Q5M7T6) V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 (D3ZIM6) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) Renin receptor × 1 (Q6AXS4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.80 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 Q6P503_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain H; PDBConstruct 1–247; UniProt 1–247

V-type proton ATPase subunit F

OrganismNot specified

UniProt P50408

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain L; UniProt 1–119 Not recorded ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit × 1 (Q5M7T6) V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 (D3ZIM6) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) Renin receptor × 1 (Q6AXS4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.80 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATF_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain L; PDBConstruct 1–119; UniProt 1–119

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain a; UniProt 1–838 Not recorded ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit F × 1 (P50408) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit × 1 (Q5M7T6) V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 (D3ZIM6) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) Renin receptor × 1 (Q6AXS4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.80 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 3
Chains and sequence ranges Author chain a; PDBConstruct 1–838; UniProt 1–838

ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a

OrganismNot specified

UniProt B0K022

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain b; UniProt 1–205 Not recorded ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit × 1 (Q5M7T6) V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 (D3ZIM6) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) Renin receptor × 1 (Q6AXS4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.80 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.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B0K022_RAT
Isoform
PDB entities 4
Chains and sequence ranges Author chain b; PDBConstruct 1–205; UniProt 1–205

V-type proton ATPase subunit S1

OrganismNot specified

UniProt O54715

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain c; UniProt 1–463 Not recorded ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit × 1 (Q5M7T6) V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 (D3ZIM6) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) Renin receptor × 1 (Q6AXS4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.80 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.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VAS1_RAT
Isoform
PDB entities 5
Chains and sequence ranges Author chain c; PDBConstruct 1–463; UniProt 1–463

V-type proton ATPase subunit

OrganismNot specified

UniProt Q5M7T6

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain d; UniProt 1–351 Not recorded ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 (D3ZIM6) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) Renin receptor × 1 (Q6AXS4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.80 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 Q5M7T6_RAT
Isoform
PDB entities 6
Chains and sequence ranges Author chain d; PDBConstruct 1–351; UniProt 1–351

V-type proton ATPase subunit e 2

OrganismNot specified

UniProt Q5EB76

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain e; UniProt 1–81 Not recorded ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit × 1 (Q5M7T6) Ribonuclease K × 1 (D3ZIM6) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) Renin receptor × 1 (Q6AXS4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.80 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.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VA0E2_RAT
Isoform
PDB entities 7
Chains and sequence ranges Author chain e; PDBConstruct 1–81; UniProt 1–81

Ribonuclease K

OrganismNot specified

UniProt D3ZIM6

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain f; UniProt 1–98 Not recorded ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit × 1 (Q5M7T6) V-type proton ATPase subunit e 2 × 1 (Q5EB76) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) Renin receptor × 1 (Q6AXS4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.80 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name D3ZIM6_RAT
Isoform
PDB entities 8
Chains and sequence ranges Author chain f; PDBConstruct 1–98; UniProt 1–98

V-type proton ATPase 16 kDa proteolipid subunit

OrganismNot specified

UniProt P63081

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain g; UniProt 1–155 Chain h; UniProt 1–155 Chain i; UniProt 1–155 Chain j; UniProt 1–155 Chain k; UniProt 1–155 Chain l; UniProt 1–155 Chain m; UniProt 1–155 Chain n; UniProt 1–155 Chain o; UniProt 1–155 Not recorded ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit × 1 (Q5M7T6) V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 (D3ZIM6) Renin receptor × 1 (Q6AXS4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.80 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.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATL_RAT
Isoform
PDB entities 9
Chains and sequence ranges Author chain g; PDBConstruct 1–155; UniProt 1–155 Author chain h; PDBConstruct 1–155; UniProt 1–155 Author chain i; PDBConstruct 1–155; UniProt 1–155 Author chain j; PDBConstruct 1–155; UniProt 1–155 Author chain k; PDBConstruct 1–155; UniProt 1–155 Author chain l; PDBConstruct 1–155; UniProt 1–155 Author chain m; PDBConstruct 1–155; UniProt 1–155 Author chain n; PDBConstruct 1–155; UniProt 1–155 Author chain o; PDBConstruct 1–155; UniProt 1–155

Renin receptor

OrganismNot specified

UniProt Q6AXS4

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain p; UniProt 1–350 Not recorded ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase 116 kDa subunit a isoform 1 × 1 (P25286) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit × 1 (Q5M7T6) V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 (D3ZIM6) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P63081) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.80 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.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RENR_RAT
Isoform
PDB entities 10
Chains and sequence ranges Author chain p; PDBConstruct 1–350; UniProt 1–350

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 6vqc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6vqc
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6vqc
Deposition date deposition_date2020-02-04
Structure title titleMammalian V-ATPase from rat brain membrane-embedded Vo region 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_guinier44.36
Radius of gyration Rg (electron density) rg_electron43.61
Forward intensity I(0) i01099710000.00
Molecular weight molecular_weight298090.0 kDa
Excluded volume excluded_volume382810 ų
Envelope volume envelope_volume509230 ų
Hydration-shell volume shell_volume93355 ų
Envelope diameter envelope_diameter154.6
Shell Rg shell_rg51.60
Envelope Rg envelope_rg43.18
Shape Rg shape_rg43.65
Total Rg total_rg43.83
Total atoms total_atoms20991
Residues n_residues2813
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 dmax143.1
Rg (real space) rg_real44.17
Rg uncertainty (real space) rg_real_error1.01
I(0) (real space) i0_real1.1000e+09
I(0) uncertainty (real space) i0_real_error1.8280e+07
Rg (reciprocal space) rg_reciprocal44.36
I(0) (reciprocal space) i0_reciprocal1100000000.0000
Solution quality estimate total_estimate0.8826
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary55.6
Skewness Skewness skewness0.218
Kurtosis Kurtosis kurtosis-0.346
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha122500000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.866; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.889

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6vqcL00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily10580 — ATPase, V1 complex, subunit F

8. Citations (1)

9. Files and Curves (10)