9jkb

Cryo-EM structure of the CUL1-RBX1-SKP1-FBXO4 SCF ubiquition ligase complex

Method: ELECTRON MICROSCOPY Dmax: 160.9 Å Quality: GOOD

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

F-box only protein 4

Homo sapiens

UniProt Q9UKT5

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 54–387 Chain D; UniProt 54–387 Not recorded Cullin-1 × 1 (Q13616) S-phase kinase-associated protein 1 × 1 (P63208) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 1 (P62877) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.93 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.

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

View Construct and Data Evidence
UniProt name FBX4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 3–315; UniProt 54–387 Author chain D; PDBConstruct 3–315; UniProt 54–387

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 2–776 Not recorded F-box only protein 4 × 2 (Q9UKT5) S-phase kinase-associated protein 1 × 1 (P63208) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 1 (P62877) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.93 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 2
Chains and sequence ranges Author chain A; PDBConstruct 22–796; UniProt 2–776

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 1–163 Not recorded F-box only protein 4 × 2 (Q9UKT5) Cullin-1 × 1 (Q13616) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 1 (P62877) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.93 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 B; PDBConstruct 4–166; UniProt 1–163

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain R; UniProt 16–108 Not recorded F-box only protein 4 × 2 (Q9UKT5) Cullin-1 × 1 (Q13616) S-phase kinase-associated protein 1 × 1 (P63208) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.93 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 4
Chains and sequence ranges Author chain R; PDBConstruct 4–96; UniProt 16–108

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 9jkb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9jkb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9jkb
Deposition date deposition_date2024-09-15
Structure title titleCryo-EM structure of the CUL1-RBX1-SKP1-FBXO4 SCF ubiquition ligase complex
Keywords keywordsubiquitination E3 ligase, Cryo-EM, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.60
Radius of gyration Rg (electron density) rg_electron53.82
Forward intensity I(0) i0259544000.00
Molecular weight molecular_weight135440.0 kDa
Excluded volume excluded_volume170050 ų
Envelope volume envelope_volume276800 ų
Hydration-shell volume shell_volume44163 ų
Envelope diameter envelope_diameter172.3
Shell Rg shell_rg56.48
Envelope Rg envelope_rg50.50
Shape Rg shape_rg53.83
Total Rg total_rg53.91
Total atoms total_atoms9532
Residues n_residues1179
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 dmax160.9
Rg (real space) rg_real53.84
Rg uncertainty (real space) rg_real_error1.52
I(0) (real space) i0_real2.5950e+08
I(0) uncertainty (real space) i0_real_error5.0460e+06
Rg (reciprocal space) rg_reciprocal53.36
I(0) (reciprocal space) i0_reciprocal259400000.0000
Solution quality estimate total_estimate0.8003
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary33.3
Skewness Skewness skewness0.223
Kurtosis Kurtosis kurtosis-0.891
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8362000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.890; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.731; 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)