4yz6

Crystal Structure of Myc3[44-238] from Arabidopsis in complex with Jaz1 peptide [200-221]

Method: X-RAY DIFFRACTION Dmax: 57.4 Å Quality: GOOD

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 44–238 Fragment:UNP residues 44-238 Protein TIFY 10A × 1 (Q9LMA8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;The MYC3(44-238)-JAZ1 complex crystals were grown at 20 degree in sitting drops containing 0.2 ul of the purified complex proteins at a concentration of 15 mg/ml and 0.2 ul of well solution containing 3.5 M sodium formate. Crystals of about 80 um in length appeared in 2 days Resolution 1.95 Å R-free 0.217

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 1–195; UniProt 44–238

Protein TIFY 10A

OrganismNot specified

UniProt Q9LMA8

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 200–221 Fragment:UNP residues 200-221 Transcription factor MYC3 × 1 (Q9FIP9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;The MYC3(44-238)-JAZ1 complex crystals were grown at 20 degree in sitting drops containing 0.2 ul of the purified complex proteins at a concentration of 15 mg/ml and 0.2 ul of well solution containing 3.5 M sodium formate. Crystals of about 80 um in length appeared in 2 days Resolution 1.95 Å R-free 0.217

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 TI10A_ARATH
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–22; UniProt 200–221

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 4yz6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4yz6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4yz6
Deposition date deposition_date2015-03-24
Structure title titleCrystal Structure of Myc3[44-238] from Arabidopsis in complex with Jaz1 peptide [200-221]
Keywords keywordsJasmonate signaling pathway, Myc3 transcription factor, Jaz1 repressor, plant transcriptional regulation, TRANSCRIPTION REGULATOR; TRANSCRIPTION REGULATOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.05
Radius of gyration Rg (electron density) rg_electron16.61
Forward intensity I(0) i09077980.00
Molecular weight molecular_weight21574.0 kDa
Excluded volume excluded_volume26731 ų
Envelope volume envelope_volume30971 ų
Hydration-shell volume shell_volume15799 ų
Envelope diameter envelope_diameter58.6
Shell Rg shell_rg22.60
Envelope Rg envelope_rg17.03
Shape Rg shape_rg16.60
Total Rg total_rg17.63
Total atoms total_atoms1522
Residues n_residues193
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 dmax57.4
Rg (real space) rg_real17.95
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real9.0780e+06
I(0) uncertainty (real space) i0_real_error1.1750e+05
Rg (reciprocal space) rg_reciprocal17.96
I(0) (reciprocal space) i0_reciprocal9078000.0000
Solution quality estimate total_estimate0.8956
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.3
Skewness Skewness skewness0.184
Kurtosis Kurtosis kurtosis-0.396
Angular range angular_range— – 0.4400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1521000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.885; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)