8u17

The ternary complex structure of DDB1-CRBN-SALL4(ZF1,2)-long bound to Pomalidomide

Method: X-RAY DIFFRACTION Dmax: 162.3 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 DNA damage-binding protein 1 × 1 (Q16531) Sal-like protein 4 × 1 (Q9UJQ4) ZN ZINC ION × 3 Y70 S-Pomalidomide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.2M Sodium malonate, 20% PEG 3350 Resolution 3.10 Å R-free 0.346
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 70–442 Not recorded DNA damage-binding protein 1 × 1 (Q16531) Sal-like protein 4 × 1 (Q9UJQ4) ZN ZINC ION × 3 Y70 S-Pomalidomide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.2M Sodium malonate, 20% PEG 3350 Resolution 3.10 Å R-free 0.346

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

DNA damage-binding protein 1

Homo sapiens

UniProt Q16531

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 B; UniProt 1–395 Chain B; UniProt 706–1140 Not recorded Protein cereblon × 1 (Q96SW2) Sal-like protein 4 × 1 (Q9UJQ4) ZN ZINC ION × 3 Y70 S-Pomalidomide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.2M Sodium malonate, 20% PEG 3350 Resolution 3.10 Å R-free 0.346
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 1–395 Chain E; UniProt 706–1140 Not recorded Protein cereblon × 1 (Q96SW2) Sal-like protein 4 × 1 (Q9UJQ4) ZN ZINC ION × 3 Y70 S-Pomalidomide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.2M Sodium malonate, 20% PEG 3350 Resolution 3.10 Å R-free 0.346

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.

202 other PDB entries and 289 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DDB1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–395; UniProt 1–395 Author chain B; PDBConstruct 402–836; UniProt 706–1140 Author chain E; PDBConstruct 1–395; UniProt 1–395 Author chain E; PDBConstruct 402–836; UniProt 706–1140

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 370–454 Not recorded Protein cereblon × 1 (Q96SW2) DNA damage-binding protein 1 × 1 (Q16531) ZN ZINC ION × 3 Y70 S-Pomalidomide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.2M Sodium malonate, 20% PEG 3350 Resolution 3.10 Å R-free 0.346
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 370–454 Not recorded Protein cereblon × 1 (Q96SW2) DNA damage-binding protein 1 × 1 (Q16531) ZN ZINC ION × 3 Y70 S-Pomalidomide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.2M Sodium malonate, 20% PEG 3350 Resolution 3.10 Å R-free 0.346

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 2–86; UniProt 370–454 Author chain F; PDBConstruct 2–86; UniProt 370–454

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 8u17

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8u17
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8u17
Deposition date deposition_date2023-08-30
Structure title titleThe ternary complex structure of DDB1-CRBN-SALL4(ZF1,2)-long bound to Pomalidomide
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_guinier48.52
Radius of gyration Rg (electron density) rg_electron48.05
Forward intensity I(0) i0896282000.00
Molecular weight molecular_weight241860.0 kDa
Excluded volume excluded_volume299060 ų
Envelope volume envelope_volume443360 ų
Hydration-shell volume shell_volume76471 ų
Envelope diameter envelope_diameter163.4
Shell Rg shell_rg52.83
Envelope Rg envelope_rg47.01
Shape Rg shape_rg48.07
Total Rg total_rg48.18
Total atoms total_atoms17033
Residues n_residues2379
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 dmax162.3
Rg (real space) rg_real48.46
Rg uncertainty (real space) rg_real_error1.50
I(0) (real space) i0_real8.9630e+08
I(0) uncertainty (real space) i0_real_error1.6410e+07
Rg (reciprocal space) rg_reciprocal48.52
I(0) (reciprocal space) i0_reciprocal896300000.0000
Solution quality estimate total_estimate0.8915
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary60.9
Skewness Skewness skewness0.231
Kurtosis Kurtosis kurtosis-0.569
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha160500000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.903; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.880

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)