SAXSdb — 8uah

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

F-box/LRR-repeat protein 17

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 310–701	Fragment：UNP residues 310-701	Transcription regulator protein BACH1 × 1 （O14867）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.30 Å

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 8UAH	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6W66 The structure of the F64A, S172A mutant Keap1-BTB domain in complex with SKP1-FBXL17 Deposited 2020-03-16	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 310–701（392 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；well solution 37.5 ul of 50 mM MgCl2, 100 mM HEPES pH 7.5, 30% (v/v) PEG MME 550 (E7 Hampton Index) + 12.5ul H2O mixed 1:1 with complex at 15mg/ml in 150 mM NaCl, 25 mM Tris/HCl pH 8.0	Resolution 3.21 Å R-free 0.290
6WCQ Structure of a substrate-bound DQC ubiquitin ligase Deposited 2020-03-31	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 310–701（392 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 8.50 Å
8UBT Structure of SCF-FBXL17-BACH1BTB E3 ligase complex Deposited 2023-09-24	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 310–701（392 aa） Fragment：UNP residues 310-701	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 mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain D 310–701（392 aa） Fragment：UNP residues 310-701 Chain K 310–701（392 aa） Fragment：UNP residues 310-701	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 mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 310–701（392 aa） Fragment：UNP residues 310-701 Chain H 310–701（392 aa） Fragment：UNP residues 310-701	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

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

View Construct and Data Evidence

UniProt name	FXL17_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain B； PDBConstruct 1–392； UniProt 310–701

Transcription regulator protein BACH1

Homo sapiens

UniProt O14867

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 7–132	Fragment：BTB domain (UNP residues 7-132)	F-box/LRR-repeat protein 17 × 1 （Q9UF56）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.30 Å

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 8UAH	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 mutation/modification Different oligomeric state Different ligand/ion 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 construct Different mutation/modification Different oligomeric state Different experimental method 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 construct Different mutation/modification Different oligomeric state Different experimental method 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 experimental method 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 construct Different mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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
8UBT Structure of SCF-FBXL17-BACH1BTB E3 ligase complex Deposited 2023-09-24	Different construct Different oligomeric state 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 construct Different mutation/modification Different oligomeric state Different experimental method 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 construct Different mutation/modification Different oligomeric state Different experimental method 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 construct Different mutation/modification Different oligomeric state Different experimental method 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
9GRA Homodimer of BACH1 BTB domain in complex with 2-Methyl-2,4-pentanediol Deposited 2024-09-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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	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

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	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–126； UniProt 7–132

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	8uah
Deposition date deposition_date	2023-09-21
Structure title title	Structure of BACH1 BTB domain-bound FBXL17 ubiquitin ligase
Keywords keywords	F-box protein, FBXO22, BACH1, LIGASE; LIGASE
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	24.90 Å
Radius of gyration Rg (electron density) rg_electron	24.02 Å
Forward intensity I(0) i0	41000900.00
Molecular weight molecular_weight	50437.0 kDa
Excluded volume excluded_volume	63611 Å³
Envelope volume envelope_volume	80564 Å³
Hydration-shell volume shell_volume	27759 Å³
Envelope diameter envelope_diameter	82.8 Å
Shell Rg shell_rg	31.36 Å
Envelope Rg envelope_rg	24.09 Å
Shape Rg shape_rg	24.01 Å
Total Rg total_rg	24.94 Å
Total atoms total_atoms	3534
Residues n_residues	451
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	94.0 Å
Rg (real space) rg_real	24.76 Å
Rg uncertainty (real space) rg_real_error	0.97 Å
I(0) (real space) i0_real	4.1000e+07
I(0) uncertainty (real space) i0_real_error	6.8280e+05
Rg (reciprocal space) rg_reciprocal	24.79 Å
I(0) (reciprocal space) i0_reciprocal	41000000.0000
Solution quality estimate total_estimate	0.7417
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	4
Primary peak position r_peak_primary	32.8 Å
Skewness Skewness skewness	0.149
Kurtosis Kurtosis kurtosis	-0.557
Angular range angular_range	— – 0.3200 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	15080000.0000
Real-space data points n_real_points	64
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.600; Stabil: 0.992; Sysdev: 1.000; Positv: 1.000; Valcen: 0.863; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	F-box/LRR-repeat protein 17
Molecular weight formula_weight	44505.5 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B
Atom count atom_count	3534

CHREPPPETPDINQLPPSILLKIFSNLSLDERCLSASLVCKYWRDLCLDFQFWKQLDLSSRQQVTDELLEKIASRSQNIIEINISDCRSMSDNGVCVLAFKCPGLLRYTAYRCKQLSDTSIIAVASHCPLLQKVHVGNQDKLTDEGLKQLGSKCRELKDIHFGQCYKISDEGMIVIAKGCLKLQRIYMQENKLVTDQSVKAFAEHCPELQYVGFMGCSVTSKGVIHLTKLRNLSSLDLRHITELDNETVMEIVKRCKNLSSLNLCLNWIINDRCVEVIAKEGQNLKELYLVSCKITDYALIAIGRYSMTIETVDVGWCKEITDQGATLIAQSSKSLRYLGLMRCDKVNEVTVEQLVQQYPHITFSTVLQDCKRTLERAYQMGWTPNMSAASS

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	Trichoplusia ni

Entity 2 Entity 2 polymer

Description description	Transcription regulator protein BACH1
Molecular weight formula_weight	14344.4 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

SVFAYESSVHSTNVLLSLNDQRKKDVLCDVTIFVEGQRFRAHRSVLAACSSYFHSRIVGQADGELNITLPEEVTVKGFEPLIQFAYTAKLILSKENVDEVCKCVEFLSVHNIEESCFQFLKFKFLD

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

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	—

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

Resolution resolution	3.30 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	198895

fit	/app/data/saxs_computation/ua/8uah/8uah.fit
pddf	/app/data/pr_computation/ua/8uah/8uah.pr.out
profile	/app/data/saxs_computation/ua/8uah/8uah.dat

Structure of BACH1 BTB domain-bound FBXL17 ubiquitin ligase

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

F-box/LRR-repeat protein 17

State in the Current Structure

Other States of the Same Protein in the Database

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)