SAXSdb — 1bx9

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

GLUTATHIONE S-TRANSFERASE

OrganismNot specified

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 2–212	Not recorded	FOE-4053-glutathione conjugate GGL-FOE-GLY × 2	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7；pH 7.00	Resolution 2.60 Å R-free 0.248

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 1BX9	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1GNW STRUCTURE OF GLUTATHIONE S-TRANSFERASE Deposited 1996-09-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–211（211 aa） Chain B 1–211（211 aa）	Not recorded	GTX S-HEXYLGLUTATHIONE × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å
5A4U AtGSTF2 from Arabidopsis thaliana in complex with indole-3-aldehyde Deposited 2015-06-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–212（212 aa） Chain B 1–212（212 aa） Chain C 1–212（212 aa） Chain D 1–212（212 aa） Chain E 1–212（212 aa） Chain F 1–212（212 aa）	Not recorded	I3A 1H-INDOLE-3-CARBALDEHYDE × 8 ACT ACETATE ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；0.1M PCTP (PROPIONIC ACID, CACODYLATE, BIS-TRIS PROPANE SYSTEM, 15% (W/V) PEG 1.5K PH 7.0. PROTEIN AT 10 MG PER ML	Resolution 2.00 Å R-free 0.234
5A4V AtGSTF2 from Arabidopsis thaliana in complex with quercetin Deposited 2015-06-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–212（212 aa） Chain B 1–212（212 aa） Chain C 1–212（212 aa） Chain D 1–212（212 aa） Chain E 1–212（212 aa） Chain F 1–212（212 aa）	Not recorded	ACT ACETATE ION × 6 QUE 3,5,7,3',4'-PENTAHYDROXYFLAVONE × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；0.1 M PTCP (PROPIONIC ACID, CACODYLATE, BIS-TRIS PROPANE SYSTEM), 15% PEG 1.5K, PROTEIN AT 10 MG PER ML, pH 7	Resolution 2.38 Å R-free 0.245
5A4W AtGSTF2 from Arabidopsis thaliana in complex with quercetrin Deposited 2015-06-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–212（212 aa） Chain B 1–212（212 aa） Chain C 1–212（212 aa） Chain D 1–212（212 aa） Chain E 1–212（212 aa） Chain F 1–212（212 aa）	Not recorded	QCT 2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4-oxo-4H-chromen-3-yl 6-deoxy-alpha-L-mannopyranoside × 8 ACT ACETATE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；0.1 M PTPC (PROPIONIC ACID, CACODYLATE, BIS-TRIS PROPANE SYSTEM), 15% PEG 1.5K; 10 MG PER ML PROTEIN, pH 7	Resolution 2.25 Å R-free 0.242
5A5K AtGSTF2 from Arabidopsis thaliana in complex with camalexin Deposited 2015-06-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain C 1–212（212 aa） Chain K 1–212（212 aa） Chain M 1–212（212 aa） Chain P 1–212（212 aa） Chain R 1–212（212 aa） Chain T 1–212（212 aa）	Not recorded	7WB (2Z)-2-indol-3-ylidene-3H-1,3-thiazole × 6	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；0.2 M SODIUM ACETATE AND 20% (W/V) PEG 3350; PH 7.0; PROTEIN AT 10 MG PER ML	Resolution 2.77 Å R-free 0.284
5A5K AtGSTF2 from Arabidopsis thaliana in complex with camalexin Deposited 2015-06-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–212（212 aa） Chain B 1–212（212 aa） Chain I 1–212（212 aa） Chain J 1–212（212 aa） Chain L 1–212（212 aa） Chain S 1–212（212 aa）	Not recorded	7WB (2Z)-2-indol-3-ylidene-3H-1,3-thiazole × 6	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；0.2 M SODIUM ACETATE AND 20% (W/V) PEG 3350; PH 7.0; PROTEIN AT 10 MG PER ML	Resolution 2.77 Å R-free 0.284
5A5K AtGSTF2 from Arabidopsis thaliana in complex with camalexin Deposited 2015-06-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain E 1–212（212 aa） Chain O 1–212（212 aa） Chain U 1–212（212 aa） Chain V 1–212（212 aa） Chain W 1–212（212 aa） Chain X 1–212（212 aa）	Not recorded	7WB (2Z)-2-indol-3-ylidene-3H-1,3-thiazole × 6	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；0.2 M SODIUM ACETATE AND 20% (W/V) PEG 3350; PH 7.0; PROTEIN AT 10 MG PER ML	Resolution 2.77 Å R-free 0.284
5A5K AtGSTF2 from Arabidopsis thaliana in complex with camalexin Deposited 2015-06-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain D 1–212（212 aa） Chain F 1–212（212 aa） Chain G 1–212（212 aa） Chain H 1–212（212 aa） Chain N 1–212（212 aa） Chain Q 1–212（212 aa）	Not recorded	7WB (2Z)-2-indol-3-ylidene-3H-1,3-thiazole × 6	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；0.2 M SODIUM ACETATE AND 20% (W/V) PEG 3350; PH 7.0; PROTEIN AT 10 MG PER ML	Resolution 2.77 Å R-free 0.284

5 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	GTH4_ARATH
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–211； UniProt 2–212

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	1bx9
Deposition date deposition_date	1998-10-14
Structure title title	GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH HERBICIDE
Keywords keywords	HERBICIDE, FOE-4053-glutathione conjugate, product of the detoxifying reaction, TRANSFERASE, TRANSFERASE-PEPTIDE COMPLEX; TRANSFERASE/PEPTIDE
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	18.46 Å
Radius of gyration Rg (electron density) rg_electron	17.35 Å
Forward intensity I(0) i0	10181800.00
Molecular weight molecular_weight	24423.0 kDa
Excluded volume excluded_volume	30884 Å³
Envelope volume envelope_volume	34738 Å³
Hydration-shell volume shell_volume	16857 Å³
Envelope diameter envelope_diameter	59.9 Å
Shell Rg shell_rg	23.42 Å
Envelope Rg envelope_rg	17.61 Å
Shape Rg shape_rg	17.34 Å
Total Rg total_rg	18.36 Å
Total atoms total_atoms	1727
Residues n_residues	211
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	58.9 Å
Rg (real space) rg_real	18.38 Å
Rg uncertainty (real space) rg_real_error	0.23 Å
I(0) (real space) i0_real	1.0180e+07
I(0) uncertainty (real space) i0_real_error	1.2140e+05
Rg (reciprocal space) rg_reciprocal	18.39 Å
I(0) (reciprocal space) i0_reciprocal	10180000.0000
Solution quality estimate total_estimate	0.6676
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	22.6 Å
Skewness Skewness skewness	0.189
Kurtosis Kurtosis kurtosis	-0.437
Angular range angular_range	— – 0.4300 Å⁻¹
Current regularization parameter α current_alpha	0.0014
Highest regularization parameter α highest_alpha	1817000.0000
Real-space data points n_real_points	74
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.893; Stabil: 1.000; Sysdev: 0.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.998

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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	GLUTATHIONE S-TRANSFERASE
Molecular weight formula_weight	24031.4 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1797

AGIKVFGHPASIATRRVLIALHEKNLDFELVHVELKDGEHKKEPFLSRNPFGQVPAFEDGDLKLFESRAITQYIAHRYENQGTNLLQTDSKNISQYAIMAIGMQVEDHQFDPVASKLAFEQIFKSIYGLTTDEAVVAEEEAKLAKVLDVYEARLKEFKYLAGETFTLTDLHHIPAIQYLLGTPTKKLFTERPRVNEWVAEITKRPASEKVQ

Entity 2 Entity 2 polymer

Description description	FOE-4053-glutathione conjugate GGL-FOE-GLY
Molecular weight formula_weight	500.5 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

ECG

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	70

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1bx9a1
Class class	a — All alpha proteins
Fold Fold fold	a.45 — GST C-terminal domain-like
Superfamily Superfamily superfamily	a.45.1 — GST C-terminal domain-like
Family Family family	a.45.1.1 — Glutathione S-transferase (GST), C-terminal domain

Domain ID domain_id	d1bx9a2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.47 — Thioredoxin fold
Superfamily Superfamily superfamily	c.47.1 — Thioredoxin-like
Family Family family	c.47.1.5 — Glutathione S-transferase (GST), N-terminal domain

CATH v4.4 (2 domains)

Domain ID domain_id	1bx9A01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	30 — Glutaredoxin
Homologous superfamily homologous superfamily	10 — Glutaredoxin

Domain ID domain_id	1bx9A02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1050 — Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
Homologous superfamily homologous superfamily	10 —

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8. Citations (1)

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Unit-cell length a length_a	59.000 Å
Unit-cell length b length_b	88.830 Å
Unit-cell length c length_c	89.850 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	2.600 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.1960
R_work r_work	0.1960
R_free r_free	0.2480

fit	/app/data/saxs_computation/bx/1bx9/1bx9.fit
pddf	/app/data/pr_computation/bx/1bx9/1bx9.pr.out
profile	/app/data/saxs_computation/bx/1bx9/1bx9.dat

GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH HERBICIDE

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

GLUTATHIONE S-TRANSFERASE

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

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)