9nn1

Yeast V1-ATPase bound to Rtc5p

Method: ELECTRON MICROSCOPY Dmax: 191.6 Å Quality: GOOD

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

H(+)-transporting two-sector ATPase

OrganismNot specified

UniProt B3LH69

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 1–617 Chain C; UniProt 1–617 Chain E; UniProt 1–617 Not recorded V-type proton ATPase subunit E × 3 (P22203) Yeast V-ATPase subunit G × 3 V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) Restriction of telomere capping protein 5 × 1 (B3LJG1) V-type proton ATPase subunit B × 3 (P16140) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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 B3LH69_YEAS1
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

V-type proton ATPase subunit E

OrganismNot specified

UniProt P22203

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 1–233 Chain I; UniProt 1–233 Chain K; UniProt 1–233 Not recorded H(+)-transporting two-sector ATPase × 3 (B3LH69) Yeast V-ATPase subunit G × 3 V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) Restriction of telomere capping protein 5 × 1 (B3LJG1) V-type proton ATPase subunit B × 3 (P16140) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

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

View Construct and Data Evidence
UniProt name VATE_YEAST
Isoform
PDB entities 2
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 D

OrganismNot specified

UniProt P32610

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 1–256 Not recorded H(+)-transporting two-sector ATPase × 3 (B3LH69) V-type proton ATPase subunit E × 3 (P22203) Yeast V-ATPase subunit G × 3 V-type proton ATPase subunit F × 1 (P39111) Restriction of telomere capping protein 5 × 1 (B3LJG1) V-type proton ATPase subunit B × 3 (P16140) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

19 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATD_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain M; PDBConstruct 1–256; UniProt 1–256

V-type proton ATPase subunit F

OrganismNot specified

UniProt P39111

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 1–118 Not recorded H(+)-transporting two-sector ATPase × 3 (B3LH69) V-type proton ATPase subunit E × 3 (P22203) Yeast V-ATPase subunit G × 3 V-type proton ATPase subunit D × 1 (P32610) Restriction of telomere capping protein 5 × 1 (B3LJG1) V-type proton ATPase subunit B × 3 (P16140) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

19 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATF_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain N; PDBConstruct 1–118; UniProt 1–118

Restriction of telomere capping protein 5

Saccharomyces cerevisiae

UniProt B3LJG1

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 R; UniProt 1–567 Mutation:N-terminal His tag H(+)-transporting two-sector ATPase × 3 (B3LH69) V-type proton ATPase subunit E × 3 (P22203) Yeast V-ATPase subunit G × 3 V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) V-type proton ATPase subunit B × 3 (P16140) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RTC5_YEAS1
Isoform
PDB entities 6
Chains and sequence ranges Author chain R; PDBConstruct 1–567; UniProt 1–567

V-type proton ATPase subunit B

OrganismNot specified

UniProt P16140

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 1–517 Chain D; UniProt 1–517 Chain F; UniProt 1–517 Not recorded H(+)-transporting two-sector ATPase × 3 (B3LH69) V-type proton ATPase subunit E × 3 (P22203) Yeast V-ATPase subunit G × 3 V-type proton ATPase subunit D × 1 (P32610) V-type proton ATPase subunit F × 1 (P39111) Restriction of telomere capping protein 5 × 1 (B3LJG1) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

18 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATB_YEAST
Isoform
PDB entities 7
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

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 9nn1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9nn1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9nn1
Deposition date deposition_date2025-03-04
Structure title titleYeast V1-ATPase bound to Rtc5p
Keywords keywordsVacuolar ATPase, V1-ATPase, Rtc5p, protein structure, PROTON TRANSPORT; PROTON TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier56.36
Radius of gyration Rg (electron density) rg_electron56.15
Forward intensity I(0) i04216860000.00
Molecular weight molecular_weight551770.0 kDa
Excluded volume excluded_volume693230 ų
Envelope volume envelope_volume1002800 ų
Hydration-shell volume shell_volume142890 ų
Envelope diameter envelope_diameter205.2
Shell Rg shell_rg62.91
Envelope Rg envelope_rg56.35
Shape Rg shape_rg56.15
Total Rg total_rg56.34
Total atoms total_atoms77843
Residues n_residues4941
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 dmax191.6
Rg (real space) rg_real56.28
Rg uncertainty (real space) rg_real_error1.73
I(0) (real space) i0_real4.2170e+09
I(0) uncertainty (real space) i0_real_error8.4710e+07
Rg (reciprocal space) rg_reciprocal56.43
I(0) (reciprocal space) i0_reciprocal4218000000.0000
Solution quality estimate total_estimate0.8510
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary68.4
Skewness Skewness skewness0.394
Kurtosis Kurtosis kurtosis-0.030
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha633600000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.753; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.821

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)