4rnd

Crystal Structure of the subunit DF-assembly of the eukaryotic V-ATPase.

Method: X-RAY DIFFRACTION Dmax: 126.0 Å Quality: REASONABLE

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

V-type proton ATPase subunit D

Saccharomyces cerevisiae S288c

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–256 Chain C; UniProt 1–256 Not recorded V-type proton ATPase subunit F × 2 (P39111) GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;291 K;0.1 M sodium citrate tribasic dehydrate, 1.2 M Ammonium citrate monobasic, ph 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.18 Å R-free 0.232

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–256; UniProt 1–256 Author chain C; PDBConstruct 1–256; UniProt 1–256

V-type proton ATPase subunit F

Saccharomyces cerevisiae S288c

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–118 Chain D; UniProt 1–118 Not recorded V-type proton ATPase subunit D × 2 (P32610) GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;291 K;0.1 M sodium citrate tribasic dehydrate, 1.2 M Ammonium citrate monobasic, ph 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.18 Å R-free 0.232

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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–118; UniProt 1–118 Author chain D; PDBConstruct 1–118; UniProt 1–118

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 4rnd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4rnd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4rnd
Deposition date deposition_date2014-10-24
Structure title titleCrystal Structure of the subunit DF-assembly of the eukaryotic V-ATPase.
Keywords keywordsalpha helical, Rossmann Fold, Hydrolase, Regulatory, Coupling; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier36.55
Radius of gyration Rg (electron density) rg_electron36.48
Forward intensity I(0) i068528200.00
Molecular weight molecular_weight66371.0 kDa
Excluded volume excluded_volume83207 ų
Envelope volume envelope_volume110530 ų
Hydration-shell volume shell_volume27184 ų
Envelope diameter envelope_diameter134.8
Shell Rg shell_rg39.33
Envelope Rg envelope_rg36.37
Shape Rg shape_rg36.50
Total Rg total_rg36.61
Total atoms total_atoms4682
Residues n_residues578
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 dmax126.0
Rg (real space) rg_real37.07
Rg uncertainty (real space) rg_real_error1.41
I(0) (real space) i0_real6.8530e+07
I(0) uncertainty (real space) i0_real_error1.2290e+06
Rg (reciprocal space) rg_reciprocal36.75
I(0) (reciprocal space) i0_reciprocal68510000.0000
Solution quality estimate total_estimate0.6832
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.4
Skewness Skewness skewness0.485
Kurtosis Kurtosis kurtosis-0.735
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24280000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.282; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.184; Smooth: 0.846

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4rndb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.149 — AtpF-like
Superfamily Superfamily superfamilyc.149.1 — AtpF-like
Family Family familyc.149.1.1 — AtpF-like
Domain ID domain_idd4rndd_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.149 — AtpF-like
Superfamily Superfamily superfamilyc.149.1 — AtpF-like
Family Family familyc.149.1.1 — AtpF-like

CATH v4.4 (2 domains)

Domain ID domain_id4rndB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily10580 — ATPase, V1 complex, subunit F
Domain ID domain_id4rndD00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily10580 — ATPase, V1 complex, subunit F

8. Citations (2)

9. Files and Curves (10)