SAXSdb — 9dt3

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

Sulfonylurea repressor EsR (L11-C6)

Escherichia coli

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–207 Chain B； UniProt 1–207	Not recorded	RXF methyl 2-[[4-ethoxy-6-(methylamino)-1,3,5-triazin-2-yl]carbamoylsulfamoyl]benzoate × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；295 K；0.05 M Magnesium chloride 0.1 M HEPES pH 7.5 30% v/v Polyethylene glycol monomethyl ether 550	Resolution 2.80 Å R-free 0.278
2	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 1–207 Chain D； UniProt 1–207	Not recorded	RXF methyl 2-[[4-ethoxy-6-(methylamino)-1,3,5-triazin-2-yl]carbamoylsulfamoyl]benzoate × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；295 K；0.05 M Magnesium chloride 0.1 M HEPES pH 7.5 30% v/v Polyethylene glycol monomethyl ether 550	Resolution 2.80 Å R-free 0.278

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.

Other PDB	Difference from Current Entry 9DT3	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2NS7 How an in vitro selected peptide mimics the antibiotic tetracycline to induce TET repressor Deposited 2006-11-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–187（187 aa） Chain B 1–187（187 aa）	Mutation：C68S, C88N, C121T, C144S Mutation：C68S, C88N, C121T, C144S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；292 K；1.4M ammonium sulfate, 0.1M sodium chloride, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.40 Å R-free 0.277
2NS7 How an in vitro selected peptide mimics the antibiotic tetracycline to induce TET repressor Deposited 2006-11-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–187（187 aa） Chain D 1–187（187 aa）	Mutation：C68S, C88N, C121T, C144S Mutation：C68S, C88N, C121T, C144S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；292 K；1.4M ammonium sulfate, 0.1M sodium chloride, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.40 Å R-free 0.277
2NS8 How an in vitro selected peptide mimics the antibiotic tetracycline to induce TET repressor Deposited 2006-11-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–187（187 aa） Chain B 1–187（187 aa）	Mutation：C68S, C88N, C121T, C144S Mutation：C68S, C88N, C121T, C144S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；292 K；4M sodium formate, 0.1M Tris-HCl, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.55 Å R-free 0.270
2NS8 How an in vitro selected peptide mimics the antibiotic tetracycline to induce TET repressor Deposited 2006-11-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–187（187 aa） Chain D 1–187（187 aa）	Mutation：C68S, C88N, C121T, C144S Mutation：C68S, C88N, C121T, C144S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；292 K；4M sodium formate, 0.1M Tris-HCl, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.55 Å R-free 0.270
2NS8 How an in vitro selected peptide mimics the antibiotic tetracycline to induce TET repressor Deposited 2006-11-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Insufficient information Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 1–187（187 aa） Chain B 1–187（187 aa） Chain C 1–187（187 aa） Chain D 1–187（187 aa）	Mutation：C68S, C88N, C121T, C144S Mutation：C68S, C88N, C121T, C144S Mutation：C68S, C88N, C121T, C144S Mutation：C68S, C88N, C121T, C144S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；292 K；4M sodium formate, 0.1M Tris-HCl, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.55 Å R-free 0.270
2VKV TetR (BD) variant L17G with reverse phenotype Deposited 2008-01-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–50（50 aa） Fragment：RESIDUES 1-50,51-208	Mutation：YES	TDC 5A,6-ANHYDROTETRACYCLINE × 2 MG MAGNESIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.7；277 K；0.1 M TRIS-HCL (PH 8.7), 0.3 M MGCL2, 20 % PEG 4000, 3 % DIOXANE, AT 277 K	Resolution 1.74 Å R-free 0.225
2XGC Crystal structure of a designed heterodimeric variant T-A(I)B of the tetracycline repressor Deposited 2010-06-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–50（50 aa） Fragment：RESIDUES 1-50,51-208	Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.15 Å R-free 0.271
2XGC Crystal structure of a designed heterodimeric variant T-A(I)B of the tetracycline repressor Deposited 2010-06-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 1–50（50 aa） Fragment：RESIDUES 1-50,51-208	Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.15 Å R-free 0.271
2XGD Crystal structure of a designed homodimeric variant T-A(L)A(L) of the tetracycline repressor Deposited 2010-06-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–50（50 aa） Fragment：RESIDUES 1-50,51-208	Mutation：YES	CL CHLORIDE ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.25 Å R-free 0.259
2XGE Crystal structure of a designed heterodimeric variant T-A(A)B of the tetracycline repressor Deposited 2010-06-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–50（50 aa） Fragment：RESIDUES 1-50,51-208	Not recorded	EDO 1,2-ETHANEDIOL × 2 NA SODIUM ION × 2 CL CHLORIDE ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.14 Å R-free 0.260
2XGE Crystal structure of a designed heterodimeric variant T-A(A)B of the tetracycline repressor Deposited 2010-06-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 1–50（50 aa） Fragment：RESIDUES 1-50,51-208	Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.14 Å R-free 0.260
3FK6 Crystal structure of TetR triple mutant (H64K, S135L, S138I) Deposited 2008-12-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–50（50 aa） Fragment：DNA-binding domain (residues 1-50) and the effector-binding domain (residues 51-208) Chain B 1–50（50 aa） Fragment：DNA-binding domain (residues 1-50) and the effector-binding domain (residues 51-208)	Mutation：H64K, S135L, S138I Mutation：H64K, S135L, S138I	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；292 K；1M dipotassium hydrogen phosphate, 200mM sodium chloride, 50mM Tris-HCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.10 Å R-free 0.262
3FK7 Crystal structure of TetR triple mutant (H64K, S135L, S138I) in complex with 4-ddma-atc Deposited 2008-12-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–50（50 aa） Fragment：DNA-binding domain (residues 1-50) and the effector-binding domain (residues 51-208) Chain B 1–50（50 aa） Fragment：DNA-binding domain (residues 1-50) and the effector-binding domain (residues 51-208)	Mutation：H64K, S135L, S138I Mutation：H64K, S135L, S138I	MG MAGNESIUM ION × 2 4DM (4aS,12aS)-3,10,11,12a-tetrahydroxy-6-methyl-1,12-dioxo-1,4,4a,5,12,12a-hexahydrotetracene-2-carboxamide × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；292 K；1M dipotassium hydrogen phosphate, 200mM sodium chloride, 50mM Tris-HCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.06 Å R-free 0.261
3ZQF Structure of Tetracycline repressor in complex with antiinducer peptide-TAP1 Deposited 2011-06-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–187（187 aa） Fragment：RESIDUES 1-187,188-208	Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；RESERVOIR: 3 M NACL, 0.1 M BIS-TRIS, PH 6.	Resolution 2.56 Å R-free 0.247
3ZQG Structure of Tetracycline repressor in complex with antiinducer peptide-TAP2 Deposited 2011-06-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–187（187 aa） Fragment：RESIDUES 1-187,188-208	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；RESERVOIR: 3 M NACL, 0.1 M BIS-TRIS, PH 6.5	Resolution 2.45 Å R-free 0.234
3ZQH Structure of Tetracycline repressor in complex with inducer peptide- TIP3 Deposited 2011-06-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–187（187 aa） Fragment：RESIDUES 1-187,188-208	Mutation：YES	EDO 1,2-ETHANEDIOL × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 9；0.2 M NACL, 0.1 M TRIS PH 9.0, 25% PEG 3350.	Resolution 1.60 Å R-free 0.224
3ZQI Structure of Tetracycline repressor in complex with inducer peptide- TIP2 Deposited 2011-06-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–187（187 aa） Fragment：RESIDUES 1-187,188-208 Chain B 1–187（187 aa） Fragment：RESIDUES 1-187,188-208	Mutation：YES Mutation：YES	EDO 1,2-ETHANEDIOL × 5 MG MAGNESIUM ION × 1 PG4 TETRAETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；0.2 M MAGNESIUM ACETATE, 0.1 M SODIUM CACODYLATE, PH 7.0, 20% PEG 8000.	Resolution 1.50 Å R-free 0.195
4AC0 TETR(B) IN COMPLEX WITH MINOCYCLINE AND MAGNESIUM Deposited 2011-12-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 2–203（202 aa）	Not recorded	MIY (4S,4AS,5AR,12AS)-4,7-BIS(DIMETHYLAMINO)-3,10,12,12A-TETRAHYDROXY-1,11-DIOXO-1,4,4A,5,5A,6,11,12A-OCTAHYDROTETRACENE-2- CARBOXAMIDE × 2 MG MAGNESIUM ION × 2 PO4 PHOSPHATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；pH 6.5	Resolution 2.45 Å R-free 0.294
6SY4 TetR in complex with the TetR-binding RNA-aptamer K1 Deposited 2019-09-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Homooligomer；Protein × 2 PDB declaration: trimeric	Chain A 1–203（203 aa） Chain B 1–203（203 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；4% v/v Tacsimate pH 6.0, 12% w/v PEG 3350	Resolution 2.69 Å R-free 0.246
6SY6 TetR in complex with the TetR-binding RNA-aptamer K2 Deposited 2019-09-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Homooligomer；Protein × 2 PDB declaration: trimeric	Chain A 1–203（203 aa） Chain B 1–203（203 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；15 % (v/v) pentaerythritol propoxylate (5/4 PO/OH), 0.2 M NaCl, pH 6.0, 0.1 M MES-NaOH	Resolution 2.90 Å R-free 0.288
9DT4 Crystal structure of the engineered sulfonylurea repressor CsR (L4.2-20), apo form Deposited 2024-09-30	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–207（207 aa） Chain B 1–207（207 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.2 M Sodium acetate 0.1 M TRIS hydrochloride pH 8.5 30% w/v Polyethylene glycol 4,000	Resolution 2.40 Å R-free 0.241
9DT5 Crystal structure of the engineered sulfonylurea repressor CsR (L4.2-20), bound to chlorsulfuron Deposited 2024-09-30	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–207（207 aa） Chain B 1–207（207 aa）	Not recorded	1CS 1-(2-CHLOROPHENYLSULFONYL)-3-(4-METHOXY-6-METHYL-L,3,5-TRIAZIN-2-YL)UREA × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.05 M Ammonium sulfate 0.05 M BIS-TRIS pH 6.5 30% w/v Polyethylene glycol 600	Resolution 2.00 Å R-free 0.228
9DT5 Crystal structure of the engineered sulfonylurea repressor CsR (L4.2-20), bound to chlorsulfuron Deposited 2024-09-30	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–207（207 aa） Chain D 1–207（207 aa）	Not recorded	1CS 1-(2-CHLOROPHENYLSULFONYL)-3-(4-METHOXY-6-METHYL-L,3,5-TRIAZIN-2-YL)UREA × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.05 M Ammonium sulfate 0.05 M BIS-TRIS pH 6.5 30% w/v Polyethylene glycol 600	Resolution 2.00 Å R-free 0.228

17 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TETR2_ECOLX
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–207； UniProt 1–207 Author chain B； PDBConstruct 1–207； UniProt 1–207 Author chain C； PDBConstruct 1–207； UniProt 1–207 Author chain D； PDBConstruct 1–207； UniProt 1–207

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	9dt3
Deposition date deposition_date	2024-09-30
最后修订 last_revision	2025-10-08
Structure title title	Crystal structure of the engineered sulfonylurea repressor EsR (L11-C6), bound to ethametsulfuron-methyl
Keywords keywords	repressor, transcription, TetR, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	32.75 Å
Radius of gyration Rg (electron density) rg_electron	32.38 Å
Forward intensity I(0) i0	123085000.00
Molecular weight molecular_weight	87660.0 kDa
Excluded volume excluded_volume	109600 Å³
Envelope volume envelope_volume	145600 Å³
Hydration-shell volume shell_volume	38626 Å³
Envelope diameter envelope_diameter	114.9 Å
Shell Rg shell_rg	38.28 Å
Envelope Rg envelope_rg	31.84 Å
Shape Rg shape_rg	32.45 Å
Total Rg total_rg	32.65 Å
Total atoms total_atoms	6156
Residues n_residues	770
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	108.2 Å
Rg (real space) rg_real	32.87 Å
Rg uncertainty (real space) rg_real_error	0.80 Å
I(0) (real space) i0_real	1.2310e+08
I(0) uncertainty (real space) i0_real_error	2.1140e+06
Rg (reciprocal space) rg_reciprocal	32.82 Å
I(0) (reciprocal space) i0_reciprocal	123100000.0000
Solution quality estimate total_estimate	0.8783
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	33.8 Å
Skewness Skewness skewness	0.409
Kurtosis Kurtosis kurtosis	-0.425
Angular range angular_range	— – 0.2400 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	29280000.0000
Real-space data points n_real_points	49
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.871; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.951; Smooth: 0.850

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Sulfonylurea repressor EsR (L11-C6)
Molecular weight formula_weight	23174.5 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	6169

MARLDKSKVINSALELLNEVGIEGLTTRKLAQKLGVEQPTLYWHVKNKRALLDAMAIEMLDRHATHYSPLERESWQNFLRNNAKSMRNALLSHRDGAKVCLGTGFTEQQYETAENSLAFLTQQGFSLENALYAMQAVGIYTLGCVLLDQELQVAKEERETPTTDSMPPLVRQAVELKDHQGAEPAFLFGLELIIAGLEKQLKCESGS

来源 Source

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	methyl 2-[[4-ethoxy-6-(methylamino)-1,3,5-triazin-2-yl]carbamoylsulfamoyl]benzoate
Molecular weight formula_weight	410.4 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	13

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8. Citations (1)

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Unit-cell length a length_a	65.819 Å
Unit-cell length b length_b	71.022 Å
Unit-cell length c length_c	90.526 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	92.19 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	29.842 Å
R factor r_factor	—
R_work r_work	0.1901
R_free r_free	0.2777

fit	/app/data/saxs_computation/dt/9dt3/9dt3.fit
pddf	/app/data/pr_computation/dt/9dt3/9dt3.pr.out
profile	/app/data/saxs_computation/dt/9dt3/9dt3.dat

Crystal structure of the engineered sulfonylurea repressor EsR (L11-C6), bound to ethametsulfuron-methyl

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

Sulfonylurea repressor EsR (L11-C6)

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction