8xli

Structure of the Vo sector of V-ATPase in the adult cortex and hippocampus

Method: ELECTRON MICROSCOPY Dmax: 143.2 Å Quality: GOOD

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

V-type proton ATPase 116 kDa subunit a 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 Other combination Heteromer Protein × 16 其他Polymer 4 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain a; UniProt 4–831 Not recorded 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 V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 V-type proton ATPase 16 kDa proteolipid subunit c × 9 (P63081) Renin receptor cytoplasmic fragment × 1 (Q6AXS4) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 1
Chains and sequence ranges Author chain a; PDBConstruct 1–828; UniProt 4–831

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 Other combination Heteromer Protein × 16 其他Polymer 4 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain b; UniProt 2–204 Not recorded V-type proton ATPase 116 kDa subunit a 1 × 1 (P25286) V-type proton ATPase subunit S1 × 1 (O54715) V-type proton ATPase subunit × 1 V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 V-type proton ATPase 16 kDa proteolipid subunit c × 9 (P63081) Renin receptor cytoplasmic fragment × 1 (Q6AXS4) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 2
Chains and sequence ranges Author chain b; PDBConstruct 1–203; UniProt 2–204

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 Other combination Heteromer Protein × 16 其他Polymer 4 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain c; UniProt 248–451 Not recorded V-type proton ATPase 116 kDa subunit a 1 × 1 (P25286) ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a × 1 (B0K022) V-type proton ATPase subunit × 1 V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 V-type proton ATPase 16 kDa proteolipid subunit c × 9 (P63081) Renin receptor cytoplasmic fragment × 1 (Q6AXS4) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 3
Chains and sequence ranges Author chain c; PDBConstruct 1–204; UniProt 248–451

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 Other combination Heteromer Protein × 16 其他Polymer 4 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain e; UniProt 3–79 Not recorded V-type proton ATPase 116 kDa subunit a 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 Ribonuclease K × 1 V-type proton ATPase 16 kDa proteolipid subunit c × 9 (P63081) Renin receptor cytoplasmic fragment × 1 (Q6AXS4) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 5
Chains and sequence ranges Author chain e; PDBConstruct 1–77; UniProt 3–79

V-type proton ATPase 16 kDa proteolipid subunit c

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 Other combination Heteromer Protein × 16 其他Polymer 4 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain g; UniProt 6–155 Chain h; UniProt 6–155 Chain i; UniProt 6–155 Chain j; UniProt 6–155 Chain k; UniProt 6–155 Chain l; UniProt 6–155 Chain m; UniProt 6–155 Chain n; UniProt 6–155 Chain o; UniProt 6–155 Not recorded V-type proton ATPase 116 kDa subunit a 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 V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 Renin receptor cytoplasmic fragment × 1 (Q6AXS4) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 7
Chains and sequence ranges Author chain g; PDBConstruct 1–150; UniProt 6–155 Author chain h; PDBConstruct 1–150; UniProt 6–155 Author chain i; PDBConstruct 1–150; UniProt 6–155 Author chain j; PDBConstruct 1–150; UniProt 6–155 Author chain k; PDBConstruct 1–150; UniProt 6–155 Author chain l; PDBConstruct 1–150; UniProt 6–155 Author chain m; PDBConstruct 1–150; UniProt 6–155 Author chain n; PDBConstruct 1–150; UniProt 6–155 Author chain o; PDBConstruct 1–150; UniProt 6–155

Renin receptor cytoplasmic fragment

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 Other combination Heteromer Protein × 16 其他Polymer 4 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain p; UniProt 292–340 Not recorded V-type proton ATPase 116 kDa subunit a 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 V-type proton ATPase subunit e 2 × 1 (Q5EB76) Ribonuclease K × 1 V-type proton ATPase 16 kDa proteolipid subunit c × 9 (P63081) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 8
Chains and sequence ranges Author chain p; PDBConstruct 1–49; UniProt 292–340

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 8xli

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8xli
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8xli
Deposition date deposition_date2023-12-26
Structure title titleStructure of the Vo sector of V-ATPase in the adult cortex and hippocampus
Keywords keywordsVo sector of V-ATPase, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.47
Radius of gyration Rg (electron density) rg_electron44.52
Forward intensity I(0) i01338270000.00
Molecular weight molecular_weight327060.0 kDa
Excluded volume excluded_volume418920 ų
Envelope volume envelope_volume584320 ų
Hydration-shell volume shell_volume103310 ų
Envelope diameter envelope_diameter152.4
Shell Rg shell_rg53.80
Envelope Rg envelope_rg43.78
Shape Rg shape_rg44.54
Total Rg total_rg44.83
Total atoms total_atoms23024
Residues n_residues3075
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 dmax143.2
Rg (real space) rg_real45.18
Rg uncertainty (real space) rg_real_error1.17
I(0) (real space) i0_real1.3380e+09
I(0) uncertainty (real space) i0_real_error2.4150e+07
Rg (reciprocal space) rg_reciprocal45.46
I(0) (reciprocal space) i0_reciprocal1339000000.0000
Solution quality estimate total_estimate0.8804
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary57.3
Skewness Skewness skewness0.156
Kurtosis Kurtosis kurtosis-0.376
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha143000000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.867; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.968; Smooth: 0.872

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)