8u15

The ternary complex structure of DDB1-CRBN-SALL4(ZF1,2)-short bound to CC-220

Method: X-RAY DIFFRACTION Dmax: 188.3 Å Quality: GOOD

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

Protein cereblon

Homo sapiens

UniProt Q96SW2

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 70–442 Not recorded DDB1 × 1 Sal-like protein 4 × 1 (Q9UJQ4) ZN ZINC ION × 3 8W7 (3S)-3-[4-({4-[(morpholin-4-yl)methyl]phenyl}methoxy)-1-oxo-1,3-dihydro-2H-isoindol-2-yl]piperidine-2,6-dione × 1 SO4 SULFATE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.2M Sodium malonate, 20% PEG 3350 Resolution 2.95 Å R-free 0.272
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 70–442 Not recorded DDB1 × 1 Sal-like protein 4 × 1 (Q9UJQ4) ZN ZINC ION × 3 8W7 (3S)-3-[4-({4-[(morpholin-4-yl)methyl]phenyl}methoxy)-1-oxo-1,3-dihydro-2H-isoindol-2-yl]piperidine-2,6-dione × 1 SO4 SULFATE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.2M Sodium malonate, 20% PEG 3350 Resolution 2.95 Å R-free 0.272

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.

93 other PDB entries and 140 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CRBN_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–373; UniProt 70–442 Author chain D; PDBConstruct 1–373; UniProt 70–442

Sal-like protein 4

Homo sapiens

UniProt Q9UJQ4

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 379–432 Not recorded Protein cereblon × 1 (Q96SW2) DDB1 × 1 ZN ZINC ION × 3 8W7 (3S)-3-[4-({4-[(morpholin-4-yl)methyl]phenyl}methoxy)-1-oxo-1,3-dihydro-2H-isoindol-2-yl]piperidine-2,6-dione × 1 SO4 SULFATE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.2M Sodium malonate, 20% PEG 3350 Resolution 2.95 Å R-free 0.272
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 379–432 Not recorded Protein cereblon × 1 (Q96SW2) DDB1 × 1 ZN ZINC ION × 3 8W7 (3S)-3-[4-({4-[(morpholin-4-yl)methyl]phenyl}methoxy)-1-oxo-1,3-dihydro-2H-isoindol-2-yl]piperidine-2,6-dione × 1 SO4 SULFATE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.2M Sodium malonate, 20% PEG 3350 Resolution 2.95 Å R-free 0.272

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 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SALL4_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 2–55; UniProt 379–432 Author chain F; PDBConstruct 2–55; UniProt 379–432

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 8u15

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8u15
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8u15
Deposition date deposition_date2023-08-30
Structure title titleThe ternary complex structure of DDB1-CRBN-SALL4(ZF1,2)-short bound to CC-220
Keywords keywordsComplex, glue, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier52.72
Radius of gyration Rg (electron density) rg_electron53.05
Forward intensity I(0) i0999358000.00
Molecular weight molecular_weight263950.0 kDa
Excluded volume excluded_volume330080 ų
Envelope volume envelope_volume467850 ų
Hydration-shell volume shell_volume75379 ų
Envelope diameter envelope_diameter200.9
Shell Rg shell_rg54.40
Envelope Rg envelope_rg51.81
Shape Rg shape_rg53.09
Total Rg total_rg52.98
Total atoms total_atoms18535
Residues n_residues2398
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 dmax188.3
Rg (real space) rg_real53.03
Rg uncertainty (real space) rg_real_error2.20
I(0) (real space) i0_real9.9940e+08
I(0) uncertainty (real space) i0_real_error2.1590e+07
Rg (reciprocal space) rg_reciprocal52.45
I(0) (reciprocal space) i0_reciprocal998500000.0000
Solution quality estimate total_estimate0.8387
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary50.2
Skewness Skewness skewness0.502
Kurtosis Kurtosis kurtosis-0.332
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha113600000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.738; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.949; Smooth: 0.735

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)