9m73

Crystal structure of MBP-fused BIL1/BZR1 (21-104) in complex with double-stranded DNA contaning CACATATGTG

Method: X-RAY DIFFRACTION Dmax: 129.8 Å Quality: GOOD

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

Maltodextrin-binding protein,Protein BRASSINAZOLE-RESISTANT 1

Arabidopsis thaliana

UniProt A0A4P1LXE0

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 Homooligomer Protein × 2 DNA 2 其他Polymer 2 PDB declaration: tetrameric(4) Count mismatch; review required Chain C; UniProt 3–371 Chain D; UniProt 3–371 Not recorded E-box(CATATG)-containing DNA × 2 alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;50 mM sodium cacodylate pH 6.5, 200 mM potassium chloride, 10 mM magnesium chloride and 10% (w/v) polyethylene glycol (PEG) 4000 Resolution 2.31 Å R-free 0.245
2 Insufficient information Homooligomer Protein × 2 DNA 2 其他Polymer 2 PDB declaration: tetrameric(4) Count mismatch; review required Chain A; UniProt 3–371 Chain B; UniProt 3–371 Not recorded E-box(CATATG)-containing DNA × 2 alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;50 mM sodium cacodylate pH 6.5, 200 mM potassium chloride, 10 mM magnesium chloride and 10% (w/v) polyethylene glycol (PEG) 4000 Resolution 2.31 Å R-free 0.245

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.

28 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A4P1LXE0_SERSF
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–370; UniProt 3–371 Author chain B; PDBConstruct 2–370; UniProt 3–371 Author chain C; PDBConstruct 2–370; UniProt 3–371 Author chain D; PDBConstruct 2–370; UniProt 3–371

Maltodextrin-binding protein,Protein BRASSINAZOLE-RESISTANT 1

Arabidopsis thaliana

UniProt Q8S307

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 Homooligomer Protein × 2 DNA 2 其他Polymer 2 PDB declaration: tetrameric(4) Count mismatch; review required Chain C; UniProt 22–104 Chain D; UniProt 22–104 Not recorded E-box(CATATG)-containing DNA × 2 alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;50 mM sodium cacodylate pH 6.5, 200 mM potassium chloride, 10 mM magnesium chloride and 10% (w/v) polyethylene glycol (PEG) 4000 Resolution 2.31 Å R-free 0.245
2 Insufficient information Homooligomer Protein × 2 DNA 2 其他Polymer 2 PDB declaration: tetrameric(4) Count mismatch; review required Chain A; UniProt 22–104 Chain B; UniProt 22–104 Not recorded E-box(CATATG)-containing DNA × 2 alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;50 mM sodium cacodylate pH 6.5, 200 mM potassium chloride, 10 mM magnesium chloride and 10% (w/v) polyethylene glycol (PEG) 4000 Resolution 2.31 Å R-free 0.245

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.

10 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BZR1_ARATH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 371–453; UniProt 22–104 Author chain B; PDBConstruct 371–453; UniProt 22–104 Author chain C; PDBConstruct 371–453; UniProt 22–104 Author chain D; PDBConstruct 371–453; UniProt 22–104

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 9m73

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9m73
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9m73
Deposition date deposition_date2025-03-09
Structure title titleCrystal structure of MBP-fused BIL1/BZR1 (21-104) in complex with double-stranded DNA contaning CACATATGTG
Keywords keywordsPlant-specific, DNA-biding protein, Transcription factor, BZR, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier41.23
Radius of gyration Rg (electron density) rg_electron40.89
Forward intensity I(0) i0726554000.00
Molecular weight molecular_weight212270.0 kDa
Excluded volume excluded_volume261800 ų
Envelope volume envelope_volume356420 ų
Hydration-shell volume shell_volume71607 ų
Envelope diameter envelope_diameter135.3
Shell Rg shell_rg47.34
Envelope Rg envelope_rg39.79
Shape Rg shape_rg40.89
Total Rg total_rg41.22
Total atoms total_atoms14946
Residues n_residues1805
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 dmax129.8
Rg (real space) rg_real41.06
Rg uncertainty (real space) rg_real_error0.85
I(0) (real space) i0_real7.2660e+08
I(0) uncertainty (real space) i0_real_error1.2880e+07
Rg (reciprocal space) rg_reciprocal41.23
I(0) (reciprocal space) i0_reciprocal726700000.0000
Solution quality estimate total_estimate0.8913
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary51.2
Skewness Skewness skewness0.165
Kurtosis Kurtosis kurtosis-0.441
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha57020000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.916; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.859

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)