2k88

Association of subunit d (Vma6p) and E (Vma4p) with G (Vma10p) and the NMR solution structure of subunit G (G1-59) of the Saccharomyces cerevisiae V1VO ATPase

Method: SOLUTION NMR Dmax: 101.0 Å Quality: REASONABLE

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

Vacuolar proton pump subunit G

Saccharomyces cerevisiae

UniProt P48836

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–58 Fragment:G(1-59)subunit of V1Vo ATPase No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.8;288 K;Ionic strength (raw mmCIF value) 0;Pressure AMBIENT NMR sample composition:25 mM sodium phosphate, 90% H2O/10% D2O | 90% H2O/10% D2O Resolution not provided

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.

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

View Construct and Data Evidence
UniProt name VATG_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–59; UniProt 2–58

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 2k88

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2k88
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2k88
Deposition date deposition_date2008-09-04
Structure title titleAssociation of subunit d (Vma6p) and E (Vma4p) with G (Vma10p) and the NMR solution structure of subunit G (G1-59) of the Saccharomyces cerevisiae V1VO ATPase
Keywords keywordsG subunit, V1Vo ATPase, Vma10p, Hydrogen ion transport, Hydrolase, Ion transport, Transport; HYDROLASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier24.26
Radius of gyration Rg (electron density) rg_electron24.98
Forward intensity I(0) i070833400.00
Molecular weight molecular_weight69400.0 kDa
Excluded volume excluded_volume87173 ų
Envelope volume envelope_volume35584 ų
Hydration-shell volume shell_volume12268 ų
Envelope diameter envelope_diameter105.6
Shell Rg shell_rg30.93
Envelope Rg envelope_rg30.22
Shape Rg shape_rg24.90
Total Rg total_rg25.49
Total atoms total_atoms9930
Residues n_residues600
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 dmax101.0
Rg (real space) rg_real25.18
Rg uncertainty (real space) rg_real_error1.75
I(0) (real space) i0_real7.0830e+07
I(0) uncertainty (real space) i0_real_error1.2010e+06
Rg (reciprocal space) rg_reciprocal24.97
I(0) (reciprocal space) i0_reciprocal70820000.0000
Solution quality estimate total_estimate0.6161
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary9.6
Skewness Skewness skewness0.642
Kurtosis Kurtosis kurtosis-0.406
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha34350.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.008; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.002; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2k88A00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily620 — F1F0 ATP synthase subunit B, membrane domain

8. Citations (1)

9. Files and Curves (10)