8ubu

Cryo-EM structure of dimeric SCF-FBXL17-BACH1BTB E3 ligase complex close conformation

Method: ELECTRON MICROSCOPY Dmax: 195.6 Å Quality: REASONABLE

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 13–776 Chain H; UniProt 13–776 Not recorded E3 ubiquitin-protein ligase RBX1, N-terminally processed × 2 (P62877) S-phase kinase-associated protein 1 × 2 (P63208) F-box/LRR-repeat protein 17 × 2 (Q9UF56) Transcription regulator protein BACH1 × 2 (O14867) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.60 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 Author chain H; PDBConstruct 1–764; UniProt 13–776

E3 ubiquitin-protein ligase RBX1, N-terminally processed

Homo sapiens

UniProt P62877

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain B; UniProt 16–108 Chain I; UniProt 16–108 Not recorded Cullin-1 × 2 (Q13616) S-phase kinase-associated protein 1 × 2 (P63208) F-box/LRR-repeat protein 17 × 2 (Q9UF56) Transcription regulator protein BACH1 × 2 (O14867) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.60 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.

99 other PDB entries and 107 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBX1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–93; UniProt 16–108 Author chain I; PDBConstruct 1–93; UniProt 16–108

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain C; UniProt 1–163 Chain G; UniProt 1–163 Not recorded Cullin-1 × 2 (Q13616) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 2 (P62877) F-box/LRR-repeat protein 17 × 2 (Q9UF56) Transcription regulator protein BACH1 × 2 (O14867) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.60 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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–162; UniProt 1–163 Author chain G; PDBConstruct 1–162; 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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain D; UniProt 310–701 Chain K; UniProt 310–701 Fragment:UNP residues 310-701 Cullin-1 × 2 (Q13616) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 2 (P62877) S-phase kinase-associated protein 1 × 2 (P63208) Transcription regulator protein BACH1 × 2 (O14867) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.60 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 4
Chains and sequence ranges Author chain D; PDBConstruct 1–392; UniProt 310–701 Author chain K; 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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain E; UniProt 7–128 Chain L; UniProt 7–128 Fragment:BTB domain (UNP residues 7-128) Cullin-1 × 2 (Q13616) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 2 (P62877) S-phase kinase-associated protein 1 × 2 (P63208) F-box/LRR-repeat protein 17 × 2 (Q9UF56) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.60 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 5
Chains and sequence ranges Author chain E; PDBConstruct 1–122; UniProt 7–128 Author chain L; 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 8ubu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8ubu
Deposition date deposition_date2023-09-25
Structure title titleCryo-EM structure of dimeric SCF-FBXL17-BACH1BTB E3 ligase complex close conformation
Keywords keywordsSCF, FBXL17, BACH1, F-box protein, CUL1, Cullin, E3 ligase, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier69.31
Radius of gyration Rg (electron density) rg_electron69.13
Forward intensity I(0) i01081960000.00
Molecular weight molecular_weight281330.0 kDa
Excluded volume excluded_volume353850 ų
Envelope volume envelope_volume692280 ų
Hydration-shell volume shell_volume85185 ų
Envelope diameter envelope_diameter205.6
Shell Rg shell_rg68.58
Envelope Rg envelope_rg64.60
Shape Rg shape_rg69.16
Total Rg total_rg69.02
Total atoms total_atoms19760
Residues n_residues2464
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 dmax195.6
Rg (real space) rg_real69.26
Rg uncertainty (real space) rg_real_error1.44
I(0) (real space) i0_real1.0820e+09
I(0) uncertainty (real space) i0_real_error2.2560e+07
Rg (reciprocal space) rg_reciprocal69.30
I(0) (reciprocal space) i0_reciprocal1082000000.0000
Solution quality estimate total_estimate0.6241
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary102.0
Skewness Skewness skewness0.072
Kurtosis Kurtosis kurtosis-0.801
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha45470000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 1.000; Stabil: 1.000; Sysdev: 0.038; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)