6vqa

Mammalian V-ATPase from rat brain soluble V1 region rotational state 2 with SidK and ADP (from focused refinement)

Method: ELECTRON MICROSCOPY Dmax: 170.2 Å Quality: GOOD

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

ATPase H+-transporting V1 subunit A

OrganismNot specified

UniProt D4A133

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain A; UniProt 1–617 Chain B; UniProt 1–617 Chain C; UniProt 1–617 Not recorded V-type proton ATPase subunit B, brain isoform × 3 (P62815) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit G × 3 (Q8R2H0) Effector protein SidK × 3 (Q5ZWW6) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.70 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 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name D4A133_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–617; UniProt 1–617 Author chain B; PDBConstruct 1–617; UniProt 1–617 Author chain C; PDBConstruct 1–617; UniProt 1–617

V-type proton ATPase subunit B, brain isoform

OrganismNot specified

UniProt P62815

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain D; UniProt 1–511 Chain E; UniProt 1–511 Chain F; UniProt 1–511 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit G × 3 (Q8R2H0) Effector protein SidK × 3 (Q5ZWW6) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.70 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 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATB2_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–511; UniProt 1–511 Author chain E; PDBConstruct 1–511; UniProt 1–511 Author chain F; PDBConstruct 1–511; UniProt 1–511

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain H; UniProt 1–247 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit G × 3 (Q8R2H0) Effector protein SidK × 3 (Q5ZWW6) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.70 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 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q6P503_RAT
Isoform
PDB entities 3
Chains and sequence ranges Author chain H; PDBConstruct 1–247; UniProt 1–247

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain I; UniProt 1–226 Chain J; UniProt 1–226 Chain K; UniProt 1–226 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit G × 3 (Q8R2H0) Effector protein SidK × 3 (Q5ZWW6) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.70 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 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATE1_RAT
Isoform
PDB entities 4
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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain M; UniProt 1–118 Chain N; UniProt 1–118 Chain O; UniProt 1–118 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) Effector protein SidK × 3 (Q5ZWW6) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.70 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 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8R2H0_RAT
Isoform
PDB entities 5
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

Effector protein SidK

Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)

UniProt Q5ZWW6

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain Q; UniProt 1–278 Chain R; UniProt 1–278 Chain S; UniProt 1–278 Fragment:N-terminal fragment with 3x FLAG tag ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit G × 3 (Q8R2H0) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.70 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.

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

View Construct and Data Evidence
UniProt name Q5ZWW6_LEGPH
Isoform
PDB entities 6
Chains and sequence ranges Author chain Q; PDBConstruct 2–279; UniProt 1–278 Author chain R; PDBConstruct 2–279; UniProt 1–278 Author chain S; PDBConstruct 2–279; UniProt 1–278

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 6vqa

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6vqa
Deposition date deposition_date2020-02-04
Structure title titleMammalian V-ATPase from rat brain soluble V1 region rotational state 2 with SidK and ADP (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_guinier51.70
Radius of gyration Rg (electron density) rg_electron51.24
Forward intensity I(0) i03685830000.00
Molecular weight molecular_weight514300.0 kDa
Excluded volume excluded_volume646080 ų
Envelope volume envelope_volume877990 ų
Hydration-shell volume shell_volume133320 ų
Envelope diameter envelope_diameter169.1
Shell Rg shell_rg60.79
Envelope Rg envelope_rg51.13
Shape Rg shape_rg51.23
Total Rg total_rg51.52
Total atoms total_atoms36114
Residues n_residues4578
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 dmax170.2
Rg (real space) rg_real51.48
Rg uncertainty (real space) rg_real_error1.33
I(0) (real space) i0_real3.6860e+09
I(0) uncertainty (real space) i0_real_error6.8040e+07
Rg (reciprocal space) rg_reciprocal51.87
I(0) (reciprocal space) i0_reciprocal3688000000.0000
Solution quality estimate total_estimate0.8749
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary62.4
Skewness Skewness skewness0.169
Kurtosis Kurtosis kurtosis-0.444
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha756900000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.831; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.947; Smooth: 0.929

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 9 domains

CATH v4.4 (9 domains)

Domain ID domain_id6vqaA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id6vqaA03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily100 — RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain
Domain ID domain_id6vqaB02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id6vqaB03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily100 — RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain
Domain ID domain_id6vqaC02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id6vqaC03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily100 — RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain
Domain ID domain_id6vqaD00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily12240
Domain ID domain_id6vqaE00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily12240
Domain ID domain_id6vqaF00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily12240

8. Citations (1)

9. Files and Curves (10)