7tmm

Complete V1 Complex from Saccharomyces cerevisiae

Method: ELECTRON MICROSCOPY Dmax: 189.6 Å Quality: REASONABLE

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

H(+)-transporting two-sector ATPase

OrganismNot specified

UniProt A0A6L0YX77

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain A; UniProt 1–617 Chain C; UniProt 1–617 Chain E; UniProt 1–617 Not recorded Vacuolar proton pump subunit B × 3 (A0A6A5Q585) V-ATPase subunit E × 3 (A0A6A5Q7Y8) V-type proton ATPase subunit G × 3 (A0A6L0ZI53) V-type proton ATPase subunit D × 1 (A0A6A5Q1W2) V-type proton ATPase subunit F × 1 (A0A6A5PYF6) V-type proton ATPase subunit C × 1 (A0A6A5PTP1) V-type proton ATPase subunit H × 1 (P41807) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.50 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 A0A6L0YX77_YEASX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–617; UniProt 1–617 Author chain C; PDBConstruct 1–617; UniProt 1–617 Author chain E; PDBConstruct 1–617; UniProt 1–617

Vacuolar proton pump subunit B

OrganismNot specified

UniProt A0A6A5Q585

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain B; UniProt 1–517 Chain D; UniProt 1–517 Chain F; UniProt 1–517 Not recorded H(+)-transporting two-sector ATPase × 3 (A0A6L0YX77) V-ATPase subunit E × 3 (A0A6A5Q7Y8) V-type proton ATPase subunit G × 3 (A0A6L0ZI53) V-type proton ATPase subunit D × 1 (A0A6A5Q1W2) V-type proton ATPase subunit F × 1 (A0A6A5PYF6) V-type proton ATPase subunit C × 1 (A0A6A5PTP1) V-type proton ATPase subunit H × 1 (P41807) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.50 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5Q585_YEASX
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–517; UniProt 1–517 Author chain D; PDBConstruct 1–517; UniProt 1–517 Author chain F; PDBConstruct 1–517; UniProt 1–517

V-ATPase subunit E

OrganismNot specified

UniProt A0A6A5Q7Y8

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain G; UniProt 1–233 Chain I; UniProt 1–233 Chain K; UniProt 1–233 Not recorded H(+)-transporting two-sector ATPase × 3 (A0A6L0YX77) Vacuolar proton pump subunit B × 3 (A0A6A5Q585) V-type proton ATPase subunit G × 3 (A0A6L0ZI53) V-type proton ATPase subunit D × 1 (A0A6A5Q1W2) V-type proton ATPase subunit F × 1 (A0A6A5PYF6) V-type proton ATPase subunit C × 1 (A0A6A5PTP1) V-type proton ATPase subunit H × 1 (P41807) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.50 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5Q7Y8_YEASX
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–233; UniProt 1–233 Author chain I; PDBConstruct 1–233; UniProt 1–233 Author chain K; PDBConstruct 1–233; UniProt 1–233

V-type proton ATPase subunit G

OrganismNot specified

UniProt A0A6L0ZI53

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain H; UniProt 1–114 Chain J; UniProt 1–114 Chain L; UniProt 1–114 Not recorded H(+)-transporting two-sector ATPase × 3 (A0A6L0YX77) Vacuolar proton pump subunit B × 3 (A0A6A5Q585) V-ATPase subunit E × 3 (A0A6A5Q7Y8) V-type proton ATPase subunit D × 1 (A0A6A5Q1W2) V-type proton ATPase subunit F × 1 (A0A6A5PYF6) V-type proton ATPase subunit C × 1 (A0A6A5PTP1) V-type proton ATPase subunit H × 1 (P41807) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.50 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 A0A6L0ZI53_YEASX
Isoform
PDB entities 4
Chains and sequence ranges Author chain H; PDBConstruct 1–114; UniProt 1–114 Author chain J; PDBConstruct 1–114; UniProt 1–114 Author chain L; PDBConstruct 1–114; UniProt 1–114

V-type proton ATPase subunit D

OrganismNot specified

UniProt A0A6A5Q1W2

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain M; UniProt 1–256 Not recorded H(+)-transporting two-sector ATPase × 3 (A0A6L0YX77) Vacuolar proton pump subunit B × 3 (A0A6A5Q585) V-ATPase subunit E × 3 (A0A6A5Q7Y8) V-type proton ATPase subunit G × 3 (A0A6L0ZI53) V-type proton ATPase subunit F × 1 (A0A6A5PYF6) V-type proton ATPase subunit C × 1 (A0A6A5PTP1) V-type proton ATPase subunit H × 1 (P41807) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.50 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5Q1W2_YEASX
Isoform
PDB entities 5
Chains and sequence ranges Author chain M; PDBConstruct 1–256; UniProt 1–256

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain N; UniProt 1–118 Not recorded H(+)-transporting two-sector ATPase × 3 (A0A6L0YX77) Vacuolar proton pump subunit B × 3 (A0A6A5Q585) V-ATPase subunit E × 3 (A0A6A5Q7Y8) V-type proton ATPase subunit G × 3 (A0A6L0ZI53) V-type proton ATPase subunit D × 1 (A0A6A5Q1W2) V-type proton ATPase subunit C × 1 (A0A6A5PTP1) V-type proton ATPase subunit H × 1 (P41807) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.50 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 6
Chains and sequence ranges Author chain N; PDBConstruct 1–118; UniProt 1–118

V-type proton ATPase subunit C

OrganismNot specified

UniProt A0A6A5PTP1

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain O; UniProt 1–392 Not recorded H(+)-transporting two-sector ATPase × 3 (A0A6L0YX77) Vacuolar proton pump subunit B × 3 (A0A6A5Q585) V-ATPase subunit E × 3 (A0A6A5Q7Y8) V-type proton ATPase subunit G × 3 (A0A6L0ZI53) V-type proton ATPase subunit D × 1 (A0A6A5Q1W2) V-type proton ATPase subunit F × 1 (A0A6A5PYF6) V-type proton ATPase subunit H × 1 (P41807) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.50 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 A0A6A5PTP1_YEASX
Isoform
PDB entities 7
Chains and sequence ranges Author chain O; PDBConstruct 1–392; UniProt 1–392

V-type proton ATPase subunit H

OrganismNot specified

UniProt P41807

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain P; UniProt 1–478 Not recorded H(+)-transporting two-sector ATPase × 3 (A0A6L0YX77) Vacuolar proton pump subunit B × 3 (A0A6A5Q585) V-ATPase subunit E × 3 (A0A6A5Q7Y8) V-type proton ATPase subunit G × 3 (A0A6L0ZI53) V-type proton ATPase subunit D × 1 (A0A6A5Q1W2) V-type proton ATPase subunit F × 1 (A0A6A5PYF6) V-type proton ATPase subunit C × 1 (A0A6A5PTP1) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.50 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 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATH_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain P; PDBConstruct 1–478; UniProt 1–478

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 7tmm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7tmm
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7tmm
Deposition date deposition_date2022-01-19
Structure title titleComplete V1 Complex from Saccharomyces cerevisiae
Keywords keywordsV-ATPase, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier56.58
Radius of gyration Rg (electron density) rg_electron55.24
Forward intensity I(0) i03256640000.00
Molecular weight molecular_weight475270.0 kDa
Excluded volume excluded_volume592260 ų
Envelope volume envelope_volume920130 ų
Hydration-shell volume shell_volume133290 ų
Envelope diameter envelope_diameter200.2
Shell Rg shell_rg61.11
Envelope Rg envelope_rg56.03
Shape Rg shape_rg55.39
Total Rg total_rg54.87
Total atoms total_atoms33713
Residues n_residues5236
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 dmax189.6
Rg (real space) rg_real58.13
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real3.2290e+09
I(0) uncertainty (real space) i0_real_error5.4010e+07
Rg (reciprocal space) rg_reciprocal56.63
I(0) (reciprocal space) i0_reciprocal3257000000.0000
Solution quality estimate total_estimate0.6830
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary67.7
Skewness Skewness skewness0.460
Kurtosis Kurtosis kurtosis-0.049
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha1.3290
Highest regularization parameter α highest_alpha432200000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.848; Stabil: 0.911; Sysdev: 0.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.628

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id7tmmG01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology2320 — hypothetical protein PF0899 fold
Homologous superfamily homologous superfamily30 — ATP synthase, E subunit, C-terminal
Domain ID domain_id7tmmI01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology2320 — hypothetical protein PF0899 fold
Homologous superfamily homologous superfamily30 — ATP synthase, E subunit, C-terminal
Domain ID domain_id7tmmM01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily3240

8. Citations (1)

9. Files and Curves (10)