2m41

Solution Structure of the AXH domain of Ataxin-1 in complex with ligand peptide from Capicua

Method: SOLUTION NMR Dmax: 58.3 Å Quality: GOOD

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

Protein capicua homolog

OrganismNot specified

UniProt Q96RK0

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 34–48 Fragment:Ataxin-1-binding linear motif (UNP 34-48) Ataxin-1 × 1 (P54253) SOLUTION NMR NMR measurement conditions:pH 6.8;310 K;Ionic strength (raw mmCIF value) 20;Pressure ambient NMR sample composition:0.5 mM [U-100% 13C; U-100% 15N] Ataxin-1 AXH domain, 0.6 mM CIC polypeptide, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.5 mM [U-100% 15N] Ataxin-1 AXH domain, 0.6 mM CIC polypeptide, 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.

6 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CIC_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–15; UniProt 34–48

Ataxin-1

Homo sapiens

UniProt P54253

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 566–688 Fragment:AXH domain, native residues A567-K689 Protein capicua homolog × 1 (Q96RK0) SOLUTION NMR NMR measurement conditions:pH 6.8;310 K;Ionic strength (raw mmCIF value) 20;Pressure ambient NMR sample composition:0.5 mM [U-100% 13C; U-100% 15N] Ataxin-1 AXH domain, 0.6 mM CIC polypeptide, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.5 mM [U-100% 15N] Ataxin-1 AXH domain, 0.6 mM CIC polypeptide, 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.

5 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATX1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–126; UniProt 566–688

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 2m41

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2m41
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2m41
Deposition date deposition_date2013-01-28
Structure title titleSolution Structure of the AXH domain of Ataxin-1 in complex with ligand peptide from Capicua
Keywords keywordsprotein/protein, Ataxin-1 AXH-CIC complex, TRANSCRIPTION REGULATOR; TRANSCRIPTION REGULATOR
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.09
Radius of gyration Rg (electron density) rg_electron14.68
Forward intensity I(0) i0671734000.00
Molecular weight molecular_weight228350.0 kDa
Excluded volume excluded_volume288900 ų
Envelope volume envelope_volume29530 ų
Hydration-shell volume shell_volume15197 ų
Envelope diameter envelope_diameter60.7
Shell Rg shell_rg22.41
Envelope Rg envelope_rg17.04
Shape Rg shape_rg14.67
Total Rg total_rg14.91
Total atoms total_atoms32070
Residues n_residues2070
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 dmax58.3
Rg (real space) rg_real15.04
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real6.7170e+08
I(0) uncertainty (real space) i0_real_error9.0640e+06
Rg (reciprocal space) rg_reciprocal15.05
I(0) (reciprocal space) i0_reciprocal671700000.0000
Solution quality estimate total_estimate0.8105
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.7
Skewness Skewness skewness0.222
Kurtosis Kurtosis kurtosis-0.336
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha446900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.583; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.783; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (2)

9. Files and Curves (10)