6o7u

Saccharomyces cerevisiae V-ATPase Stv1-VO

Method: ELECTRON MICROSCOPY Dmax: 133.4 Å Quality: GOOD

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

V-type proton ATPase subunit a, Golgi isoform

OrganismNot specified

UniProt P37296

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 1–890 Not recorded V0 assembly protein 1 × 1 (P53262) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit e × 1 (Q3E7B6) Putative protein YPR170W-B × 1 (P0C5R9) V-type proton ATPase subunit c × 8 (P25515) ;V-type proton ATPase subunit c' ; × 1 (P32842) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.10 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name STV1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain a; PDBConstruct 1–890; UniProt 1–890

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 b; UniProt 1–265 Not recorded V-type proton ATPase subunit a, Golgi isoform × 1 (P37296) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit e × 1 (Q3E7B6) Putative protein YPR170W-B × 1 (P0C5R9) V-type proton ATPase subunit c × 8 (P25515) ;V-type proton ATPase subunit c' ; × 1 (P32842) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.10 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 2
Chains and sequence ranges Author chain b; PDBConstruct 1–265; UniProt 1–265

;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 a, Golgi isoform × 1 (P37296) V0 assembly protein 1 × 1 (P53262) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit e × 1 (Q3E7B6) Putative protein YPR170W-B × 1 (P0C5R9) V-type proton ATPase subunit c × 8 (P25515) ;V-type proton ATPase subunit c' ; × 1 (P32842) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.10 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 3
Chains and sequence ranges Author chain c; PDBConstruct 1–213; UniProt 1–213

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 d; UniProt 1–345 Not recorded V-type proton ATPase subunit a, Golgi isoform × 1 (P37296) V0 assembly protein 1 × 1 (P53262) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V-type proton ATPase subunit e × 1 (Q3E7B6) Putative protein YPR170W-B × 1 (P0C5R9) V-type proton ATPase subunit c × 8 (P25515) ;V-type proton ATPase subunit c' ; × 1 (P32842) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.10 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 4
Chains and sequence ranges Author chain d; PDBConstruct 1–345; UniProt 1–345

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 e; UniProt 1–73 Not recorded V-type proton ATPase subunit a, Golgi isoform × 1 (P37296) V0 assembly protein 1 × 1 (P53262) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V-type proton ATPase subunit d × 1 (P32366) Putative protein YPR170W-B × 1 (P0C5R9) V-type proton ATPase subunit c × 8 (P25515) ;V-type proton ATPase subunit c' ; × 1 (P32842) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.10 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 5
Chains and sequence ranges Author chain e; PDBConstruct 1–73; UniProt 1–73

Putative protein YPR170W-B

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 f; UniProt 1–85 Not recorded V-type proton ATPase subunit a, Golgi isoform × 1 (P37296) V0 assembly protein 1 × 1 (P53262) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit e × 1 (Q3E7B6) V-type proton ATPase subunit c × 8 (P25515) ;V-type proton ATPase subunit c' ; × 1 (P32842) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.10 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 f; PDBConstruct 1–85; UniProt 1–85

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 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 Chain m; UniProt 1–160 Chain n; UniProt 1–160 Not recorded V-type proton ATPase subunit a, Golgi isoform × 1 (P37296) V0 assembly protein 1 × 1 (P53262) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit e × 1 (Q3E7B6) Putative protein YPR170W-B × 1 (P0C5R9) ;V-type proton ATPase subunit c' ; × 1 (P32842) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.10 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 7
Chains and sequence ranges 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 Author chain m; PDBConstruct 1–160; UniProt 1–160 Author chain n; PDBConstruct 1–160; UniProt 1–160

;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 o; UniProt 1–164 Not recorded V-type proton ATPase subunit a, Golgi isoform × 1 (P37296) V0 assembly protein 1 × 1 (P53262) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit e × 1 (Q3E7B6) Putative protein YPR170W-B × 1 (P0C5R9) V-type proton ATPase subunit c × 8 (P25515) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.10 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 8
Chains and sequence ranges Author chain o; PDBConstruct 1–164; UniProt 1–164

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 6o7u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6o7u
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6o7u
Deposition date deposition_date2019-03-08
Structure title titleSaccharomyces cerevisiae V-ATPase Stv1-VO
Keywords keywordsProton pump, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.44
Radius of gyration Rg (electron density) rg_electron42.59
Forward intensity I(0) i01118880000.00
Molecular weight molecular_weight302060.0 kDa
Excluded volume excluded_volume388500 ų
Envelope volume envelope_volume520980 ų
Hydration-shell volume shell_volume96261 ų
Envelope diameter envelope_diameter140.8
Shell Rg shell_rg52.05
Envelope Rg envelope_rg41.66
Shape Rg shape_rg42.59
Total Rg total_rg43.03
Total atoms total_atoms21268
Residues n_residues2832
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 dmax133.4
Rg (real space) rg_real43.14
Rg uncertainty (real space) rg_real_error1.19
I(0) (real space) i0_real1.1190e+09
I(0) uncertainty (real space) i0_real_error2.0380e+07
Rg (reciprocal space) rg_reciprocal43.44
I(0) (reciprocal space) i0_reciprocal1119000000.0000
Solution quality estimate total_estimate0.8906
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary55.6
Skewness Skewness skewness0.063
Kurtosis Kurtosis kurtosis-0.489
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha95870000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.900; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.954; Smooth: 0.919

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (19 domains)

Domain ID domain_idd6o7ud_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.40 — V-type ATP synthase subunit C
Superfamily Superfamily superfamilyf.40.1 — V-type ATP synthase subunit C
Family Family familyf.40.1.1 — V-type ATP synthase subunit C
Domain ID domain_idd6o7ug1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd6o7ug2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.0 — automated matches
Domain ID domain_idd6o7uh1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd6o7uh2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.0 — automated matches
Domain ID domain_idd6o7ui1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd6o7ui2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.0 — automated matches
Domain ID domain_idd6o7uj1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd6o7uj2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.0 — automated matches
Domain ID domain_idd6o7uk1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd6o7uk2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.0 — automated matches
Domain ID domain_idd6o7ul1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd6o7ul2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.0 — automated matches
Domain ID domain_idd6o7um1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd6o7um2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.0 — automated matches
Domain ID domain_idd6o7un1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c
Domain ID domain_idd6o7un2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.0 — automated matches
Domain ID domain_idd6o7uo1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.0 — automated matches
Domain ID domain_idd6o7uo2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id6o7uc01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily610 — lithium bound rotor ring of v- atpase

8. Citations (1)

9. Files and Curves (10)