5t0q

Crystal structure of the Myc3 N-terminal domain [44-242] in complex with JAZ10 Jas domain [166-192] from arabidopsis

Method: X-RAY DIFFRACTION Dmax: 55.1 Å Quality: EXCELLENT

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

Transcription factor MYC3

Arabidopsis thaliana

UniProt Q9FIP9

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 44–242 Not recorded Protein TIFY 9 × 1 (Q93ZM9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;20% w/v polyethylene glycol 3,350, 0.2 M magnesium formate dihydrate, pH 7.0. Resolution 2.15 Å R-free 0.242

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.

8 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYC3_ARATH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–199; UniProt 44–242

Protein TIFY 9

Arabidopsis thaliana

UniProt Q93ZM9

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 166–192 Fragment:UNP residues 166-192 Transcription factor MYC3 × 1 (Q9FIP9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;20% w/v polyethylene glycol 3,350, 0.2 M magnesium formate dihydrate, pH 7.0. Resolution 2.15 Å R-free 0.242

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TIF9_ARATH
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–27; UniProt 166–192

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 5t0q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5t0q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5t0q
Deposition date deposition_date2016-08-16
Structure title titleCrystal structure of the Myc3 N-terminal domain [44-242] in complex with JAZ10 Jas domain [166-192] from arabidopsis
Keywords keywordstranscriptional repression, jasmonate signaling, MYC3, JAZ10 CMID, alternative splicing, desensitization, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.80
Radius of gyration Rg (electron density) rg_electron16.40
Forward intensity I(0) i08703140.00
Molecular weight molecular_weight21112.0 kDa
Excluded volume excluded_volume26159 ų
Envelope volume envelope_volume30370 ų
Hydration-shell volume shell_volume15656 ų
Envelope diameter envelope_diameter55.3
Shell Rg shell_rg22.33
Envelope Rg envelope_rg16.83
Shape Rg shape_rg16.39
Total Rg total_rg17.43
Total atoms total_atoms1489
Residues n_residues188
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 dmax55.1
Rg (real space) rg_real17.70
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real8.7030e+06
I(0) uncertainty (real space) i0_real_error1.1420e+05
Rg (reciprocal space) rg_reciprocal17.71
I(0) (reciprocal space) i0_reciprocal8703000.0000
Solution quality estimate total_estimate0.9011
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.1
Skewness Skewness skewness0.185
Kurtosis Kurtosis kurtosis-0.390
Angular range angular_range— – 0.4450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1559000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.977

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)