8ua6

Cryo-EM Structure of SCF-FBOX22-BACH1BTB

Method: ELECTRON MICROSCOPY Dmax: 135.8 Å Quality: GOOD

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

F-box only protein 22

Homo sapiens

UniProt Q8NEZ5

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 1–403 Not recorded Transcription regulator protein BACH1 × 2 (O14867) S-phase kinase-associated protein 1 × 1 (P63208) Cullin-1 × 1 (Q13616) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FBX22_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 1–403; UniProt 1–403

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 7–128 Chain E; UniProt 7–128 Fragment:BTB domain (UNP residues 7-128) F-box only protein 22 × 1 (Q8NEZ5) S-phase kinase-associated protein 1 × 1 (P63208) Cullin-1 × 1 (Q13616) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

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 D; PDBConstruct 1–122; UniProt 7–128 Author chain E; PDBConstruct 1–122; UniProt 7–128

S-phase kinase-associated protein 1

Homo sapiens

UniProt P63208

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 1–160 Not recorded F-box only protein 22 × 1 (Q8NEZ5) Transcription regulator protein BACH1 × 2 (O14867) Cullin-1 × 1 (Q13616) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

71 other PDB entries and 97 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SKP1_HUMAN
Isoform P63208-2
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 1–160; UniProt 1–160

Cullin-1

Homo sapiens

UniProt Q13616

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 13–776 Not recorded F-box only protein 22 × 1 (Q8NEZ5) Transcription regulator protein BACH1 × 2 (O14867) S-phase kinase-associated protein 1 × 1 (P63208) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

47 other PDB entries and 56 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CUL1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain A; PDBConstruct 1–764; UniProt 13–776

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 8ua6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ua6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ua6
Deposition date deposition_date2023-09-20
Structure title titleCryo-EM Structure of SCF-FBOX22-BACH1BTB
Keywords keywordsF-box protein, FBXO22, BACH1, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.49
Radius of gyration Rg (electron density) rg_electron41.00
Forward intensity I(0) i0291340000.00
Molecular weight molecular_weight139460.0 kDa
Excluded volume excluded_volume174940 ų
Envelope volume envelope_volume258530 ų
Hydration-shell volume shell_volume53449 ų
Envelope diameter envelope_diameter138.4
Shell Rg shell_rg45.94
Envelope Rg envelope_rg39.78
Shape Rg shape_rg40.96
Total Rg total_rg41.44
Total atoms total_atoms9806
Residues n_residues1232
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

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

Maximum dimension Dmax dmax135.8
Rg (real space) rg_real41.47
Rg uncertainty (real space) rg_real_error1.18
I(0) (real space) i0_real2.9130e+08
I(0) uncertainty (real space) i0_real_error4.6190e+06
Rg (reciprocal space) rg_reciprocal41.49
I(0) (reciprocal space) i0_reciprocal291300000.0000
Solution quality estimate total_estimate0.8235
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.6
Skewness Skewness skewness0.252
Kurtosis Kurtosis kurtosis-0.419
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha31260000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.901; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)