4wth

Ataxin-3 Carboxy Terminal Region - Crystal C2 (triclinic)

Method: X-RAY DIFFRACTION Dmax: 146.6 Å Quality: GOOD

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

Maltose-binding periplasmic protein, Ataxin-3 chimera

Homo sapiens

UniProt P0AEY0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 27–392 Fragment:MBP residues 27-392 (UNP) + Ataxin-3 C-terminal region (UNP residues 278-324) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;24% PEG5000 MME, 0.9 M sodium acetate, 0.06 M imidazole, pH 8.0, 0.1 M zinc acetate Resolution 2.25 Å R-free 0.250
2 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 27–392 Fragment:MBP residues 27-392 (UNP) + Ataxin-3 C-terminal region (UNP residues 278-324) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;24% PEG5000 MME, 0.9 M sodium acetate, 0.06 M imidazole, pH 8.0, 0.1 M zinc acetate Resolution 2.25 Å R-free 0.250

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.

109 other PDB entries and 147 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECO57
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–366; UniProt 27–392 Author chain B; PDBConstruct 1–366; UniProt 27–392

Maltose-binding periplasmic protein, Ataxin-3 chimera

Homo sapiens

UniProt P54252

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 278–324 Fragment:MBP residues 27-392 (UNP) + Ataxin-3 C-terminal region (UNP residues 278-324) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;24% PEG5000 MME, 0.9 M sodium acetate, 0.06 M imidazole, pH 8.0, 0.1 M zinc acetate Resolution 2.25 Å R-free 0.250
2 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 278–324 Fragment:MBP residues 27-392 (UNP) + Ataxin-3 C-terminal region (UNP residues 278-324) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;24% PEG5000 MME, 0.9 M sodium acetate, 0.06 M imidazole, pH 8.0, 0.1 M zinc acetate Resolution 2.25 Å R-free 0.250

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 ATX3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 371–417; UniProt 278–324 Author chain B; PDBConstruct 371–417; UniProt 278–324

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 4wth

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4wth
Deposition date deposition_date2014-10-30
Structure title titleAtaxin-3 Carboxy Terminal Region - Crystal C2 (triclinic)
Keywords keywordsataxin-3, polyglutamine helix, nerve tissue proteins, polyQ, triplet repeat disorder, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.80
Radius of gyration Rg (electron density) rg_electron33.72
Forward intensity I(0) i0123457000.00
Molecular weight molecular_weight89548.0 kDa
Excluded volume excluded_volume112370 ų
Envelope volume envelope_volume155300 ų
Hydration-shell volume shell_volume38705 ų
Envelope diameter envelope_diameter156.3
Shell Rg shell_rg39.56
Envelope Rg envelope_rg35.43
Shape Rg shape_rg33.71
Total Rg total_rg34.23
Total atoms total_atoms6309
Residues n_residues809
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 dmax146.6
Rg (real space) rg_real35.00
Rg uncertainty (real space) rg_real_error2.13
I(0) (real space) i0_real1.2350e+08
I(0) uncertainty (real space) i0_real_error2.4580e+06
Rg (reciprocal space) rg_reciprocal34.88
I(0) (reciprocal space) i0_reciprocal123400000.0000
Solution quality estimate total_estimate0.7520
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.1
Skewness Skewness skewness0.556
Kurtosis Kurtosis kurtosis0.257
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29410000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.415; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.530; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)