8eas

Yeast VO in complex with Vma12-22p

Method: ELECTRON MICROSCOPY Dmax: 146.7 Å Quality: GOOD

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

Vacuolar ATPase assembly protein VMA22

OrganismNot specified

UniProt P38784

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain A; UniProt 1–181 Not recorded V-type proton ATPase assembly factor Vma12p × 1 V-type proton ATPase subunit F × 1 (A0A6A5PYF6) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) 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) Yeast V-ATPase subunit f × 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 Resolution 2.60 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 VMA22_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–181; UniProt 1–181

V-type proton ATPase subunit F

OrganismNot specified

UniProt A0A6A5PYF6

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain F; UniProt 1–118 Not recorded Vacuolar ATPase assembly protein VMA22 × 1 (P38784) V-type proton ATPase assembly factor Vma12p × 1 V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) 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) Yeast V-ATPase subunit f × 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 Resolution 2.60 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 A0A6A5PYF6_YEASX
Isoform
PDB entities 3
Chains and sequence ranges Author chain F; PDBConstruct 1–118; UniProt 1–118

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain a; UniProt 1–840 Not recorded Vacuolar ATPase assembly protein VMA22 × 1 (P38784) V-type proton ATPase assembly factor Vma12p × 1 V-type proton ATPase subunit F × 1 (A0A6A5PYF6) 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) Yeast V-ATPase subunit f × 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 Resolution 2.60 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 4
Chains and sequence ranges Author chain a; PDBConstruct 1–840; UniProt 1–840

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain b; UniProt 1–265 Not recorded Vacuolar ATPase assembly protein VMA22 × 1 (P38784) V-type proton ATPase assembly factor Vma12p × 1 V-type proton ATPase subunit F × 1 (A0A6A5PYF6) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit e × 1 (Q3E7B6) Yeast V-ATPase subunit f × 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 Resolution 2.60 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 5
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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain c; UniProt 1–213 Not recorded Vacuolar ATPase assembly protein VMA22 × 1 (P38784) V-type proton ATPase assembly factor Vma12p × 1 V-type proton ATPase subunit F × 1 (A0A6A5PYF6) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V0 assembly protein 1 × 1 (P53262) V-type proton ATPase subunit d × 1 (P32366) V-type proton ATPase subunit e × 1 (Q3E7B6) Yeast V-ATPase subunit f × 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 Resolution 2.60 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 6
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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain d; UniProt 1–345 Not recorded Vacuolar ATPase assembly protein VMA22 × 1 (P38784) V-type proton ATPase assembly factor Vma12p × 1 V-type proton ATPase subunit F × 1 (A0A6A5PYF6) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V0 assembly protein 1 × 1 (P53262) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V-type proton ATPase subunit e × 1 (Q3E7B6) Yeast V-ATPase subunit f × 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 Resolution 2.60 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 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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain e; UniProt 1–73 Not recorded Vacuolar ATPase assembly protein VMA22 × 1 (P38784) V-type proton ATPase assembly factor Vma12p × 1 V-type proton ATPase subunit F × 1 (A0A6A5PYF6) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) V0 assembly protein 1 × 1 (P53262) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V-type proton ATPase subunit d × 1 (P32366) Yeast V-ATPase subunit f × 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 Resolution 2.60 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 8
Chains and sequence ranges Author chain e; PDBConstruct 1–73; UniProt 1–73

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain f; UniProt 1–85 Not recorded Vacuolar ATPase assembly protein VMA22 × 1 (P38784) V-type proton ATPase assembly factor Vma12p × 1 V-type proton ATPase subunit F × 1 (A0A6A5PYF6) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) 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 Resolution 2.60 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 9
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 × 18 PDB declaration: octadecameric(18) 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 Vacuolar ATPase assembly protein VMA22 × 1 (P38784) V-type proton ATPase assembly factor Vma12p × 1 V-type proton ATPase subunit F × 1 (A0A6A5PYF6) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) 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) Yeast V-ATPase subunit f × 1 (P0C5R9) ;V-type proton ATPase subunit c' ; × 1 (P32842) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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 10
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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain o; UniProt 1–164 Not recorded Vacuolar ATPase assembly protein VMA22 × 1 (P38784) V-type proton ATPase assembly factor Vma12p × 1 V-type proton ATPase subunit F × 1 (A0A6A5PYF6) V-type proton ATPase subunit a, vacuolar isoform × 1 (P32563) 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) Yeast V-ATPase subunit f × 1 (P0C5R9) V-type proton ATPase subunit c × 8 (P25515) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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 11
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 8eas

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8eas
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8eas
Deposition date deposition_date2022-08-29
Structure title titleYeast VO in complex with Vma12-22p
Keywords keywordsV-type, ATPase, assembly, proton, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier46.58
Radius of gyration Rg (electron density) rg_electron45.97
Forward intensity I(0) i01550240000.00
Molecular weight molecular_weight352160.0 kDa
Excluded volume excluded_volume450710 ų
Envelope volume envelope_volume590930 ų
Hydration-shell volume shell_volume102900 ų
Envelope diameter envelope_diameter162.5
Shell Rg shell_rg54.03
Envelope Rg envelope_rg45.27
Shape Rg shape_rg45.98
Total Rg total_rg46.23
Total atoms total_atoms24802
Residues n_residues3280
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 dmax146.7
Rg (real space) rg_real46.36
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real1.5500e+09
I(0) uncertainty (real space) i0_real_error2.8280e+07
Rg (reciprocal space) rg_reciprocal46.58
I(0) (reciprocal space) i0_reciprocal1551000000.0000
Solution quality estimate total_estimate0.8694
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.1
Skewness Skewness skewness0.239
Kurtosis Kurtosis kurtosis-0.247
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha105200000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.875; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.957; Smooth: 0.717

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id8easo01
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 (2)

9. Files and Curves (10)