SAXSdb — 9gra

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

Transcription regulator protein BACH1

Homo sapiens

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 7–128 Chain B； UniProt 7–128	Not recorded	MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8.5；294 K；0.16 M Ammonium sulfate, 0.08 M Tris-HCl, 14.4 % (w/v) PEG3350, 6 % (v/v) MPD	Resolution 1.47 Å R-free 0.234

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 9GRA	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
29HH Cryo-EM structure of the CUL1-RBX1-SKP1-FBXO22 SCF ubiquition ligase in complex with NSD2, UNC10088 and Bach1 Deposited 2026-03-11	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain G 1–736（736 aa） Chain H 1–736（736 aa）	Not recorded	A1J20 ~{N}-cyclopropyl-~{N}-[[4-[[2-(6-oxidanylhexanoyl)-1~{H}-isoquinolin-6-yl]carbamoyl]phenyl]methyl]-3-oxidanylidene-4~{H}-1,4-benzoxazine-7-carboxamide × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.20 Å
2IHC Crystal structure of the bric-a-brac (BTB) domain of human BACH1 Deposited 2006-09-26	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 7–128（122 aa） Chain B 7–128（122 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；20 % PEG3350, 200 mM MgCl2, 0.1M Tris buffer, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.44 Å R-free 0.278
2IHC Crystal structure of the bric-a-brac (BTB) domain of human BACH1 Deposited 2006-09-26	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 7–128（122 aa） Chain D 7–128（122 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；20 % PEG3350, 200 mM MgCl2, 0.1M Tris buffer, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.44 Å R-free 0.278
2IHC Crystal structure of the bric-a-brac (BTB) domain of human BACH1 Deposited 2006-09-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 7–128（122 aa） Chain B 7–128（122 aa） Chain C 7–128（122 aa） Chain D 7–128（122 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；20 % PEG3350, 200 mM MgCl2, 0.1M Tris buffer, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.44 Å R-free 0.278
8S7D Cryo-EM structure of SKP1-FBXO22 in complex with a BACH1 BTB dimer at 3.2A resolution Deposited 2024-02-29	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 7–128（122 aa） Chain B 7–128（122 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8UA3 Cryo-EM Structure of FBOX22-BACH1BTB Deposited 2023-09-20	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 7–128（122 aa） Fragment：BTB domain (UNP residues 7-128) Chain E 7–128（122 aa） Fragment：BTB domain (UNP residues 7-128)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
8UA6 Cryo-EM Structure of SCF-FBOX22-BACH1BTB Deposited 2023-09-20	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain D 7–128（122 aa） Fragment：BTB domain (UNP residues 7-128) Chain E 7–128（122 aa） Fragment：BTB domain (UNP residues 7-128)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å
8UAH Structure of BACH1 BTB domain-bound FBXL17 ubiquitin ligase Deposited 2023-09-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 7–132（126 aa） Fragment：BTB domain (UNP residues 7-132)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
8UBT Structure of SCF-FBXL17-BACH1BTB E3 ligase complex Deposited 2023-09-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain D 7–128（122 aa） Fragment：BTB domain (UNP residues 7-128)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
8UBU Cryo-EM structure of dimeric SCF-FBXL17-BACH1BTB E3 ligase complex close conformation Deposited 2023-09-25	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain E 7–128（122 aa） Fragment：BTB domain (UNP residues 7-128) Chain L 7–128（122 aa） Fragment：BTB domain (UNP residues 7-128)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.60 Å
8UBV Cryo-EM structure of dimeric FBXL17-BACH1BTB E3 ubiquitin ligase complex Deposited 2023-09-25	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 7–128（122 aa） Fragment：BTB domain (UNP residues 7-128) Chain I 7–128（122 aa） Fragment：BTB domain (UNP residues 7-128)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.10 Å
9GP5 Homodimer of BACH1 F9A mutant BTB domain Deposited 2024-09-06	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 7–128（122 aa） Chain D 7–128（122 aa）	Mutation：F9A Mutation：F9A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；294 K；0.02 M HEPES, 0.15 M NaCl, 5% (w/v) glycerol, 0.001 M TCEP	Resolution 1.90 Å R-free 0.226
9GR9 Homodimer of BACH1 BTB domain Deposited 2024-09-11	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 7–128（122 aa） Chain B 7–128（122 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；294 K；0.1 M Tris-HCL, 0.2 M Li2SO4, 30 % (w/v) PEG4000	Resolution 2.25 Å R-free 0.246
9GR9 Homodimer of BACH1 BTB domain Deposited 2024-09-11	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 7–128（122 aa） Chain D 7–128（122 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；294 K；0.1 M Tris-HCL, 0.2 M Li2SO4, 30 % (w/v) PEG4000	Resolution 2.25 Å R-free 0.246

11 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	BACH1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–124； UniProt 7–128 Author chain B； PDBConstruct 3–124； UniProt 7–128

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	9gra
Deposition date deposition_date	2024-09-11
Structure title title	Homodimer of BACH1 BTB domain in complex with 2-Methyl-2,4-pentanediol
Keywords keywords	BACH1, back-to-back domain, BTB domain, 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	21.02 Å
Radius of gyration Rg (electron density) rg_electron	20.58 Å
Forward intensity I(0) i0	13065600.00
Molecular weight molecular_weight	27565.0 kDa
Excluded volume excluded_volume	34720 Å³
Envelope volume envelope_volume	42013 Å³
Hydration-shell volume shell_volume	18101 Å³
Envelope diameter envelope_diameter	73.5 Å
Shell Rg shell_rg	26.05 Å
Envelope Rg envelope_rg	21.06 Å
Shape Rg shape_rg	20.59 Å
Total Rg total_rg	21.37 Å
Total atoms total_atoms	1940
Residues n_residues	246
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	70.8 Å
Rg (real space) rg_real	21.13 Å
Rg uncertainty (real space) rg_real_error	0.55 Å
I(0) (real space) i0_real	1.3070e+07
I(0) uncertainty (real space) i0_real_error	1.5760e+05
Rg (reciprocal space) rg_reciprocal	21.11 Å
I(0) (reciprocal space) i0_reciprocal	13070000.0000
Solution quality estimate total_estimate	0.7749
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	21.5 Å
Skewness Skewness skewness	0.527
Kurtosis Kurtosis kurtosis	-0.151
Angular range angular_range	— – 0.3800 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3329000.0000
Real-space data points n_real_points	70
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.713; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.931; Smooth: 0.000

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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	Transcription regulator protein BACH1
Molecular weight formula_weight	14058.0 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	2339

SMSVFAYESSVHSTNVLLSLNDQRKKDVLCDVTIFVEGQRFRAHRSVLAACSSYFHSRIVGQADGELNITLPEEVTVKGFEPLIQFAYTAKLILSKENVDEVCKCVEFLSVHNIEESCFQFLKF

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	(4R)-2-METHYLPENTANE-2,4-DIOL
Molecular weight formula_weight	118.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	366

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8. Citations (1)

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Unit-cell length a length_a	31.129 Å
Unit-cell length b length_b	69.459 Å
Unit-cell length c length_c	64.867 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	91.86 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

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

Resolution resolution	1.470 Å
Low-resolution limit resolution_low	64.830 Å
R factor r_factor	0.1970
R_work r_work	0.1951
R_free r_free	0.2344

fit	/app/data/saxs_computation/gr/9gra/9gra.fit
pddf	/app/data/pr_computation/gr/9gra/9gra.pr.out
profile	/app/data/saxs_computation/gr/9gra/9gra.dat

Homodimer of BACH1 BTB domain in complex with 2-Methyl-2,4-pentanediol

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

Transcription regulator protein BACH1

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