7tap

Cryo-EM structure of archazolid A bound to yeast VO V-ATPase

Method: ELECTRON MICROSCOPY Dmax: 133.2 Å Quality: GOOD

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

;V-type proton ATPase subunit c' ;

OrganismNot specified

UniProt P32842

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain D; UniProt 1–164 Not recorded ;V-type proton ATPase subunit c'' ; × 1 (P23968) V0 assembly protein 1 × 1 (P53262) V-type proton ATPase subunit e × 1 (Q3E7B6) V-type proton ATPase subunit c × 8 (P25515) Yeast V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) KJL Archazolid A × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

29 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATL2_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain D; PDBConstruct 1–164; UniProt 1–164

;V-type proton ATPase subunit c'' ;

OrganismNot specified

UniProt P23968

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain C; UniProt 1–213 Not recorded ;V-type proton ATPase subunit c' ; × 1 (P32842) V0 assembly protein 1 × 1 (P53262) V-type proton ATPase subunit e × 1 (Q3E7B6) V-type proton ATPase subunit c × 8 (P25515) Yeast V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) KJL Archazolid A × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

29 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATO_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–213; UniProt 1–213

V0 assembly protein 1

OrganismNot specified

UniProt P53262

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain N; UniProt 1–265 Not recorded ;V-type proton ATPase subunit c' ; × 1 (P32842) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V-type proton ATPase subunit e × 1 (Q3E7B6) V-type proton ATPase subunit c × 8 (P25515) Yeast V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) KJL Archazolid A × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

25 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VOA1_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain N; PDBConstruct 1–265; UniProt 1–265

V-type proton ATPase subunit e

OrganismNot specified

UniProt Q3E7B6

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain M; UniProt 1–73 Not recorded ;V-type proton ATPase subunit c' ; × 1 (P32842) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V0 assembly protein 1 × 1 (P53262) V-type proton ATPase subunit c × 8 (P25515) Yeast V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) KJL Archazolid A × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VA0E_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain M; PDBConstruct 1–73; UniProt 1–73

V-type proton ATPase subunit c

OrganismNot specified

UniProt P25515

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain E; UniProt 1–160 Chain F; UniProt 1–160 Chain G; UniProt 1–160 Chain H; UniProt 1–160 Chain I; UniProt 1–160 Chain J; UniProt 1–160 Chain K; UniProt 1–160 Chain L; UniProt 1–160 Not recorded ;V-type proton ATPase subunit c' ; × 1 (P32842) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V0 assembly protein 1 × 1 (P53262) V-type proton ATPase subunit e × 1 (Q3E7B6) Yeast V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) KJL Archazolid A × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

32 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATL1_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–160; UniProt 1–160 Author chain F; PDBConstruct 1–160; UniProt 1–160 Author chain G; PDBConstruct 1–160; UniProt 1–160 Author chain H; PDBConstruct 1–160; UniProt 1–160 Author chain I; PDBConstruct 1–160; UniProt 1–160 Author chain J; PDBConstruct 1–160; UniProt 1–160 Author chain K; PDBConstruct 1–160; UniProt 1–160 Author chain L; PDBConstruct 1–160; UniProt 1–160

Yeast V-ATPase subunit f

OrganismNot specified

UniProt P0C5R9

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain O; UniProt 1–85 Not recorded ;V-type proton ATPase subunit c' ; × 1 (P32842) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V0 assembly protein 1 × 1 (P53262) V-type proton ATPase subunit e × 1 (Q3E7B6) V-type proton ATPase subunit c × 8 (P25515) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) KJL Archazolid A × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

24 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name YP17B_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain O; PDBConstruct 1–85; UniProt 1–85

V-type proton ATPase subunit d

OrganismNot specified

UniProt P32366

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain B; UniProt 1–345 Not recorded ;V-type proton ATPase subunit c' ; × 1 (P32842) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V0 assembly protein 1 × 1 (P53262) V-type proton ATPase subunit e × 1 (Q3E7B6) V-type proton ATPase subunit c × 8 (P25515) Yeast V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) KJL Archazolid A × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

32 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VA0D_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain B; PDBConstruct 1–345; UniProt 1–345

V-type proton ATPase subunit a, vacuolar isoform

OrganismNot specified

UniProt P32563

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain A; UniProt 1–840 Not recorded ;V-type proton ATPase subunit c' ; × 1 (P32842) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V0 assembly protein 1 × 1 (P53262) V-type proton ATPase subunit e × 1 (Q3E7B6) V-type proton ATPase subunit c × 8 (P25515) Yeast V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit d × 1 (P32366) KJL Archazolid A × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

31 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPH1_YEAST
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 7tap

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7tap
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7tap
Deposition date deposition_date2021-12-21
Structure title titleCryo-EM structure of archazolid A bound to yeast VO V-ATPase
Keywords keywordsinhibitor, complex, proton pump, 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_guinier43.38
Radius of gyration Rg (electron density) rg_electron42.59
Forward intensity I(0) i01233670000.00
Molecular weight molecular_weight319800.0 kDa
Excluded volume excluded_volume411940 ų
Envelope volume envelope_volume527440 ų
Hydration-shell volume shell_volume97204 ų
Envelope diameter envelope_diameter142.2
Shell Rg shell_rg52.28
Envelope Rg envelope_rg41.71
Shape Rg shape_rg42.60
Total Rg total_rg42.98
Total atoms total_atoms22520
Residues n_residues2915
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 dmax133.2
Rg (real space) rg_real43.08
Rg uncertainty (real space) rg_real_error0.95
I(0) (real space) i0_real1.2340e+09
I(0) uncertainty (real space) i0_real_error2.0890e+07
Rg (reciprocal space) rg_reciprocal43.37
I(0) (reciprocal space) i0_reciprocal1234000000.0000
Solution quality estimate total_estimate0.8899
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary55.5
Skewness Skewness skewness0.069
Kurtosis Kurtosis kurtosis-0.489
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha93770000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.901; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.955; Smooth: 0.906

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)