4ys9

Ataxin-3 Carboxy-Terminal Region - Crystal C1 (tetragonal)

Method: X-RAY DIFFRACTION Dmax: 68.7 Å Quality: EXCELLENT

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 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 × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;278 K;25% PEG5000 MME, 1.0 M sodium acetate, 0.1 M imidazole, pH 8.0, 0.1 M zinc acetate Resolution 2.00 Å R-free 0.223

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 148 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 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 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 × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;278 K;25% PEG5000 MME, 1.0 M sodium acetate, 0.1 M imidazole, pH 8.0, 0.1 M zinc acetate Resolution 2.00 Å R-free 0.223

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 7 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 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 4ys9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4ys9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4ys9
Deposition date deposition_date2015-03-16
Structure title titleAtaxin-3 Carboxy-Terminal Region - Crystal C1 (tetragonal)
Keywords keywords;Ataxin-3, Polyglutamine, Huntington's Disease, Triplet repeat disorder, ataxins, ataxia, TRANSCRIPTION ;; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.14
Radius of gyration Rg (electron density) rg_electron20.95
Forward intensity I(0) i029475900.00
Molecular weight molecular_weight42661.0 kDa
Excluded volume excluded_volume53736 ų
Envelope volume envelope_volume62655 ų
Hydration-shell volume shell_volume24476 ų
Envelope diameter envelope_diameter71.5
Shell Rg shell_rg28.03
Envelope Rg envelope_rg21.18
Shape Rg shape_rg20.89
Total Rg total_rg22.05
Total atoms total_atoms3002
Residues n_residues384
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 dmax68.7
Rg (real space) rg_real22.01
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real2.9480e+07
I(0) uncertainty (real space) i0_real_error3.9530e+05
Rg (reciprocal space) rg_reciprocal22.04
I(0) (reciprocal space) i0_reciprocal29480000.0000
Solution quality estimate total_estimate0.9045
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.6
Skewness Skewness skewness0.200
Kurtosis Kurtosis kurtosis-0.452
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7026000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.921; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4ys9b_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamilyc.94.1 — Periplasmic binding protein-like II
Family Family familyc.94.1.1 — Phosphate binding protein-like

8. Citations (1)

9. Files and Curves (10)