8ubt

Structure of SCF-FBXL17-BACH1BTB E3 ligase complex

Method: ELECTRON MICROSCOPY Dmax: 141.3 Å Quality: GOOD

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

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 13–776 Fragment:UNP residues 310-701 S-phase kinase-associated protein 1 × 1 (P63208) F-box/LRR-repeat protein 17 × 1 (Q9UF56) Transcription regulator protein BACH1 × 1 (O14867) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–764; UniProt 13–776

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–163 Fragment:BTB domain (UNP residues 7-128) Cullin-1 × 1 (Q13616) F-box/LRR-repeat protein 17 × 1 (Q9UF56) Transcription regulator protein BACH1 × 1 (O14867) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–163; UniProt 1–163

F-box/LRR-repeat protein 17

Homo sapiens

UniProt Q9UF56

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 C; UniProt 310–701 Fragment:UNP residues 310-701 Cullin-1 × 1 (Q13616) S-phase kinase-associated protein 1 × 1 (P63208) Transcription regulator protein BACH1 × 1 (O14867) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

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 3
Chains and sequence ranges Author chain C; 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 7–128 Fragment:BTB domain (UNP residues 7-128) Cullin-1 × 1 (Q13616) S-phase kinase-associated protein 1 × 1 (P63208) F-box/LRR-repeat protein 17 × 1 (Q9UF56) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 4
Chains and sequence ranges Author chain D; PDBConstruct 1–122; 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.

SAXS scattering curve SAXS Profile

SAXS profile for 8ubt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8ubt
Deposition date deposition_date2023-09-24
Structure title titleStructure of SCF-FBXL17-BACH1BTB E3 ligase complex
Keywords keywordsSCF, FBXL17, BACH1, F-box protein, E3 ligase, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.55
Radius of gyration Rg (electron density) rg_electron42.21
Forward intensity I(0) i0224754000.00
Molecular weight molecular_weight123120.0 kDa
Excluded volume excluded_volume154700 ų
Envelope volume envelope_volume236770 ų
Hydration-shell volume shell_volume48512 ų
Envelope diameter envelope_diameter143.3
Shell Rg shell_rg46.10
Envelope Rg envelope_rg40.54
Shape Rg shape_rg42.19
Total Rg total_rg42.51
Total atoms total_atoms8642
Residues n_residues1082
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 dmax141.3
Rg (real space) rg_real42.57
Rg uncertainty (real space) rg_real_error1.24
I(0) (real space) i0_real2.2480e+08
I(0) uncertainty (real space) i0_real_error4.1030e+06
Rg (reciprocal space) rg_reciprocal42.55
I(0) (reciprocal space) i0_reciprocal224700000.0000
Solution quality estimate total_estimate0.8867
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.5
Skewness Skewness skewness0.249
Kurtosis Kurtosis kurtosis-0.534
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12020000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.908; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.821

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)