9det

Human V-ATPase Vo subcomplex (containing subunit isoform a4) bound to nanobody and inhibitor

Method: ELECTRON MICROSCOPY Dmax: 159.6 Å Quality: REASONABLE

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

V-type proton ATPase subunit e 1

OrganismNot specified

UniProt O15342

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 × 17 PDB declaration: 17-meric(17) Consistent with protein copy count Chain e; UniProt 1–81 Not recorded Ribonuclease kappa × 1 (Q6P5S7) V-type proton ATPase subunit S1 × 1 (Q15904) Renin receptor × 1 (O75787) V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q99437) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P27449) V-type proton ATPase subunit d 1 × 1 (P61421) V-type proton ATPase 116 kDa subunit a 4 × 1 (Q9HBG4) Anti V-ATPase Nanobody 2CAS66 × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 CLR CHOLESTEROL × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 3 A1A4Q Cladoniamide A × 9 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2;20 mM Tris, 150 mM NaCl, 0.5 mM EDTA, 2 mM DTT, pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VA0E1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain e; PDBConstruct 1–81; UniProt 1–81

Ribonuclease kappa

OrganismNot specified

UniProt Q6P5S7

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 × 17 PDB declaration: 17-meric(17) Consistent with protein copy count Chain f; UniProt 1–137 Not recorded V-type proton ATPase subunit e 1 × 1 (O15342) V-type proton ATPase subunit S1 × 1 (Q15904) Renin receptor × 1 (O75787) V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q99437) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P27449) V-type proton ATPase subunit d 1 × 1 (P61421) V-type proton ATPase 116 kDa subunit a 4 × 1 (Q9HBG4) Anti V-ATPase Nanobody 2CAS66 × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 CLR CHOLESTEROL × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 3 A1A4Q Cladoniamide A × 9 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2;20 mM Tris, 150 mM NaCl, 0.5 mM EDTA, 2 mM DTT, pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RNK_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain f; PDBConstruct 1–137; UniProt 1–137

V-type proton ATPase subunit S1

OrganismNot specified

UniProt Q15904

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 × 17 PDB declaration: 17-meric(17) Consistent with protein copy count Chain o; UniProt 1–470 Not recorded V-type proton ATPase subunit e 1 × 1 (O15342) Ribonuclease kappa × 1 (Q6P5S7) Renin receptor × 1 (O75787) V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q99437) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P27449) V-type proton ATPase subunit d 1 × 1 (P61421) V-type proton ATPase 116 kDa subunit a 4 × 1 (Q9HBG4) Anti V-ATPase Nanobody 2CAS66 × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 CLR CHOLESTEROL × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 3 A1A4Q Cladoniamide A × 9 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2;20 mM Tris, 150 mM NaCl, 0.5 mM EDTA, 2 mM DTT, pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VAS1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain o; PDBConstruct 1–470; UniProt 1–470

Renin receptor

OrganismNot specified

UniProt O75787

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 × 17 PDB declaration: 17-meric(17) Consistent with protein copy count Chain p; UniProt 1–350 Not recorded V-type proton ATPase subunit e 1 × 1 (O15342) Ribonuclease kappa × 1 (Q6P5S7) V-type proton ATPase subunit S1 × 1 (Q15904) V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q99437) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P27449) V-type proton ATPase subunit d 1 × 1 (P61421) V-type proton ATPase 116 kDa subunit a 4 × 1 (Q9HBG4) Anti V-ATPase Nanobody 2CAS66 × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 CLR CHOLESTEROL × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 3 A1A4Q Cladoniamide A × 9 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2;20 mM Tris, 150 mM NaCl, 0.5 mM EDTA, 2 mM DTT, pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 RENR_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain p; PDBConstruct 1–350; UniProt 1–350

V-type proton ATPase 21 kDa proteolipid subunit

OrganismNot specified

UniProt Q99437

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 × 17 PDB declaration: 17-meric(17) Consistent with protein copy count Chain b; UniProt 1–205 Not recorded V-type proton ATPase subunit e 1 × 1 (O15342) Ribonuclease kappa × 1 (Q6P5S7) V-type proton ATPase subunit S1 × 1 (Q15904) Renin receptor × 1 (O75787) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P27449) V-type proton ATPase subunit d 1 × 1 (P61421) V-type proton ATPase 116 kDa subunit a 4 × 1 (Q9HBG4) Anti V-ATPase Nanobody 2CAS66 × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 CLR CHOLESTEROL × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 3 A1A4Q Cladoniamide A × 9 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2;20 mM Tris, 150 mM NaCl, 0.5 mM EDTA, 2 mM DTT, pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATO_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain b; PDBConstruct 1–205; UniProt 1–205

V-type proton ATPase 16 kDa proteolipid subunit

OrganismNot specified

UniProt P27449

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 × 17 PDB declaration: 17-meric(17) Consistent with protein copy count Chain c; UniProt 1–155 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 Not recorded V-type proton ATPase subunit e 1 × 1 (O15342) Ribonuclease kappa × 1 (Q6P5S7) V-type proton ATPase subunit S1 × 1 (Q15904) Renin receptor × 1 (O75787) V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q99437) V-type proton ATPase subunit d 1 × 1 (P61421) V-type proton ATPase 116 kDa subunit a 4 × 1 (Q9HBG4) Anti V-ATPase Nanobody 2CAS66 × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 CLR CHOLESTEROL × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 3 A1A4Q Cladoniamide A × 9 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2;20 mM Tris, 150 mM NaCl, 0.5 mM EDTA, 2 mM DTT, pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATL_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain c; PDBConstruct 1–155; UniProt 1–155 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

V-type proton ATPase subunit d 1

OrganismNot specified

UniProt P61421

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 × 17 PDB declaration: 17-meric(17) Consistent with protein copy count Chain d; UniProt 1–351 Not recorded V-type proton ATPase subunit e 1 × 1 (O15342) Ribonuclease kappa × 1 (Q6P5S7) V-type proton ATPase subunit S1 × 1 (Q15904) Renin receptor × 1 (O75787) V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q99437) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P27449) V-type proton ATPase 116 kDa subunit a 4 × 1 (Q9HBG4) Anti V-ATPase Nanobody 2CAS66 × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 CLR CHOLESTEROL × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 3 A1A4Q Cladoniamide A × 9 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2;20 mM Tris, 150 mM NaCl, 0.5 mM EDTA, 2 mM DTT, pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VA0D1_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain d; PDBConstruct 1–351; UniProt 1–351

V-type proton ATPase 116 kDa subunit a 4

Homo sapiens

UniProt Q9HBG4

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 × 17 PDB declaration: 17-meric(17) Consistent with protein copy count Chain a; UniProt 1–840 Not recorded V-type proton ATPase subunit e 1 × 1 (O15342) Ribonuclease kappa × 1 (Q6P5S7) V-type proton ATPase subunit S1 × 1 (Q15904) Renin receptor × 1 (O75787) V-type proton ATPase 21 kDa proteolipid subunit × 1 (Q99437) V-type proton ATPase 16 kDa proteolipid subunit × 9 (P27449) V-type proton ATPase subunit d 1 × 1 (P61421) Anti V-ATPase Nanobody 2CAS66 × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 CLR CHOLESTEROL × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 3 A1A4Q Cladoniamide A × 9 WJP methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2;20 mM Tris, 150 mM NaCl, 0.5 mM EDTA, 2 mM DTT, pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 VPP4_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain a; PDBConstruct 1–840; UniProt 1–840

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 9det

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9det
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9det
Deposition date deposition_date2024-08-29
Structure title titleHuman V-ATPase Vo subcomplex (containing subunit isoform a4) bound to nanobody and inhibitor
Keywords keywordsV-ATPase, lipid nanodisc, Vo subcomplex, inhibitor, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.61
Radius of gyration Rg (electron density) rg_electron46.51
Forward intensity I(0) i01552310000.00
Molecular weight molecular_weight356500.0 kDa
Excluded volume excluded_volume457520 ų
Envelope volume envelope_volume628080 ų
Hydration-shell volume shell_volume107660 ų
Envelope diameter envelope_diameter172.2
Shell Rg shell_rg54.94
Envelope Rg envelope_rg45.60
Shape Rg shape_rg46.39
Total Rg total_rg47.29
Total atoms total_atoms50652
Residues n_residues3209
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 dmax159.6
Rg (real space) rg_real47.35
Rg uncertainty (real space) rg_real_error1.17
I(0) (real space) i0_real1.5520e+09
I(0) uncertainty (real space) i0_real_error2.6110e+07
Rg (reciprocal space) rg_reciprocal47.61
I(0) (reciprocal space) i0_reciprocal1553000000.0000
Solution quality estimate total_estimate0.6361
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary58.0
Skewness Skewness skewness0.227
Kurtosis Kurtosis kurtosis-0.256
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha155100000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.776; Stabil: 1.000; Sysdev: 0.006; Positv: 1.000; Valcen: 0.968; Smooth: 0.952

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

8. Citations (1)

9. Files and Curves (10)