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7tq1

Crystal structure of adaptive laboratory evolved sulfonamide-resistant Dihydropteroate Synthase (DHPS) from Escherichia coli in complex with 6-hydroxymethylpterin

Method: X-RAY DIFFRACTION Dmax: 94.6 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Dihydropteroate synthase

Escherichia coli

UniProt P0AC13

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 1–282 Not recorded HHR 6-HYDROXYMETHYLPTERIN × 2 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8.5；298 K；25% (w/v) PEG 3350, 0.2 M magnesium chloride, 0.1 M Tris pH 8.5, 2 mM 6-hydroxymethyl- 7,8-dihydropterin diphosphate + 2mM para-aminobenzoic acid Resolution 2.73 Å R-free 0.288
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain B； UniProt 1–282 Not recorded HHR 6-HYDROXYMETHYLPTERIN × 2 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8.5；298 K；25% (w/v) PEG 3350, 0.2 M magnesium chloride, 0.1 M Tris pH 8.5, 2 mM 6-hydroxymethyl- 7,8-dihydropterin diphosphate + 2mM para-aminobenzoic acid Resolution 2.73 Å R-free 0.288

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 7TQ1 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1AJ0 CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF E. COLI DIHYDROPTEROATE SYNTHASE Deposited 1997-05-14 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–282（282 aa）
Not recorded SO4 SULFATE ION × 1 PH2 2-AMINO-6-HYDROXYMETHYL-7,8-DIHYDRO-3H-PTERIDIN-4-ONE × 1 SAN SULFANILAMIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.4；PROTEIN WAS CRYSTALLIZED FROM 42% AMMONIUM SULFATE, 50MM TRIS-HCL, PH 8.4.
Resolution 2.00 Å
1AJ2 CRYSTAL STRUCTURE OF A BINARY COMPLEX OF E. COLI DIHYDROPTEROATE SYNTHASE Deposited 1997-05-14 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–282（282 aa）
Not recorded SO4 SULFATE ION × 1 2PH [7,8-DIHYDRO-PTERIN-6-YL METHANYL]-PHOSPHONOPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.4；PROTEIN WAS CRYSTALLIZED FROM 42% AMMONIUM SULFATE, 50MM TRIS-HCL, PH 8.4.
Resolution 2.00 Å
1AJZ STRUCTURE OF DIHYDROPTEROATE PYROPHOSPHORYLASE Deposited 1997-05-13 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–282（282 aa）
Not recorded SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.4；PROTEIN WAS CRYSTALLIZED FROM 42% AMMONIUM SULFATE, 50MM TRIS-HCL, PH 8.4.
Resolution 2.00 Å
9P4A E. coli Dihydropteroate Synthase in complex with pterin-based inhibitor Deposited 2025-06-16 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 1–282（282 aa）
Chain B 1–282（282 aa）
Not recorded A1CG3 (2S)-2-(7-amino-4,5-dioxo-1,4,5,6-tetrahydropyrimido[4,5-c]pyridazin-3-yl)propanoic acid × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293.15 K；50 mM Tris, 32-50% Ammonium Sulfate
Resolution 3.00 Å R-free 0.337
9P5I E. coli Dihydropteroate Synthase in complex with pterin-based inhibitor Deposited 2025-06-18 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 1–275（275 aa）
Chain B 1–275（275 aa）
Not recorded A1CG7 7-amino-1-methyl-3-{[(1H-tetrazol-5-yl)amino]methyl}pyrimido[4,5-c]pyridazine-4,5(1H,6H)-dione × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293.15 K；50 mM Tris, 32-50% Ammonium Sulfate
Resolution 2.14 Å R-free 0.238

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DHPS_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 2–285； UniProt 1–282 Author chain B； PDBConstruct 2–285； UniProt 1–282

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 7tq1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7tq1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7tq1
Deposition date deposition_date2022-01-26
Structure title titleCrystal structure of adaptive laboratory evolved sulfonamide-resistant Dihydropteroate Synthase (DHPS) from Escherichia coli in complex with 6-hydroxymethylpterin
Keywords keywords;DHPS, DIHYDROPTEROATE SYNTHASE, FOLP, TIM BARREL, ALPHA BETA PROTEIN, SULFONAMIDES, STRUCTURAL GENOMICS, CSGID, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, NIAID, NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES, TRANSFERASE, IDP98884 ;; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier28.49 Å
Radius of gyration Rg (electron density) rg_electron27.99 Å
Forward intensity I(0) i058396900.00
Molecular weight molecular_weight59154.0 kDa
Excluded volume excluded_volume73968 ų
Envelope volume envelope_volume92613 ų
Hydration-shell volume shell_volume28397 ų
Envelope diameter envelope_diameter97.1 Å
Shell Rg shell_rg34.27 Å
Envelope Rg envelope_rg28.03 Å
Shape Rg shape_rg28.00 Å
Total Rg total_rg28.61 Å
Total atoms total_atoms4152
Residues n_residues541
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax94.6 Å
Rg (real space) rg_real28.66 Å
Rg uncertainty (real space) rg_real_error0.75 Å
I(0) (real space) i0_real5.8400e+07
I(0) uncertainty (real space) i0_real_error8.9260e+05
Rg (reciprocal space) rg_reciprocal28.61 Å
I(0) (reciprocal space) i0_reciprocal58390000.0000
Solution quality estimate total_estimate0.8617
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary92.9 Å
Skewness Skewness skewness0.432
Kurtosis Kurtosis kurtosis-0.505
Angular range angular_range— – 0.2800 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17060000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.801; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.872; Smooth: 0.925
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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8. Citations (1)

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9. Files and Curves (10)