7fdm

Crystal structure of transcription factor MYB29 in complex with MYC3

Method: X-RAY DIFFRACTION Dmax: 73.7 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 Not recorded Transcription factor MYB29 × 1 (Q9FLR1) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.1 M HEPES pH 7.0, 20% (w/v) PEG 6000, 0.2 M Sodium chloride Resolution 2.50 Å R-free 0.268
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 44–238 Not recorded Transcription factor MYB29 × 1 (Q9FLR1) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.1 M HEPES pH 7.0, 20% (w/v) PEG 6000, 0.2 M Sodium chloride Resolution 2.50 Å R-free 0.268

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 12 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 Author chain B; PDBConstruct 1–195; UniProt 44–238

Transcription factor MYB29

Arabidopsis thaliana

UniProt Q9FLR1

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 C; UniProt 174–222 Not recorded Transcription factor MYC3 × 1 (Q9FIP9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.1 M HEPES pH 7.0, 20% (w/v) PEG 6000, 0.2 M Sodium chloride Resolution 2.50 Å R-free 0.268
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 174–222 Not recorded Transcription factor MYC3 × 1 (Q9FIP9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.1 M HEPES pH 7.0, 20% (w/v) PEG 6000, 0.2 M Sodium chloride Resolution 2.50 Å R-free 0.268

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name MYB29_ARATH
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–49; UniProt 174–222 Author chain D; PDBConstruct 1–49; UniProt 174–222

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 7fdm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7fdm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7fdm
Deposition date deposition_date2021-07-17
Structure title titleCrystal structure of transcription factor MYB29 in complex with MYC3
Keywords keywordsTranscription factor complex, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.64
Radius of gyration Rg (electron density) rg_electron21.58
Forward intensity I(0) i029327900.00
Molecular weight molecular_weight40536.0 kDa
Excluded volume excluded_volume50230 ų
Envelope volume envelope_volume61267 ų
Hydration-shell volume shell_volume23587 ų
Envelope diameter envelope_diameter72.5
Shell Rg shell_rg28.50
Envelope Rg envelope_rg21.52
Shape Rg shape_rg21.58
Total Rg total_rg22.40
Total atoms total_atoms2856
Residues n_residues372
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 dmax73.7
Rg (real space) rg_real22.57
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real2.9330e+07
I(0) uncertainty (real space) i0_real_error4.2150e+05
Rg (reciprocal space) rg_reciprocal22.59
I(0) (reciprocal space) i0_reciprocal29330000.0000
Solution quality estimate total_estimate0.8951
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.8
Skewness Skewness skewness0.262
Kurtosis Kurtosis kurtosis-0.381
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8006000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.880; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)