9hne

Cereblon in complex with DDB1, GSPT1 and Compound-1

Method: X-RAY DIFFRACTION Dmax: 213.1 Å Quality: GOOD

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

Eukaryotic peptide chain release factor GTP-binding subunit ERF3A

Homo sapiens

UniProt P15170

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 300–496 Not recorded DNA damage-binding protein 1 × 1 (Q16531) Protein cereblon × 1 (Q96SW2) ZN ZINC ION × 1 A1IWG 2-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-6-fluoranyl-1-oxidanylidene-3~{H}-isoindole-5-carboxylic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;292 K;0.2 M Sodium citrate, 0.1 M Bis-Tris propane pH 7.5, 20% w/v PEG 3350 Resolution 3.90 Å R-free 0.336
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 300–496 Not recorded DNA damage-binding protein 1 × 1 (Q16531) Protein cereblon × 1 (Q96SW2) ZN ZINC ION × 1 A1IWG 2-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-6-fluoranyl-1-oxidanylidene-3~{H}-isoindole-5-carboxylic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;292 K;0.2 M Sodium citrate, 0.1 M Bis-Tris propane pH 7.5, 20% w/v PEG 3350 Resolution 3.90 Å R-free 0.336

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.

6 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ERF3A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–197; UniProt 300–496 Author chain D; PDBConstruct 1–197; UniProt 300–496

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 1–1140 Not recorded Eukaryotic peptide chain release factor GTP-binding subunit ERF3A × 1 (P15170) Protein cereblon × 1 (Q96SW2) ZN ZINC ION × 1 A1IWG 2-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-6-fluoranyl-1-oxidanylidene-3~{H}-isoindole-5-carboxylic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;292 K;0.2 M Sodium citrate, 0.1 M Bis-Tris propane pH 7.5, 20% w/v PEG 3350 Resolution 3.90 Å R-free 0.336
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 1–1140 Not recorded Eukaryotic peptide chain release factor GTP-binding subunit ERF3A × 1 (P15170) Protein cereblon × 1 (Q96SW2) ZN ZINC ION × 1 A1IWG 2-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-6-fluoranyl-1-oxidanylidene-3~{H}-isoindole-5-carboxylic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;292 K;0.2 M Sodium citrate, 0.1 M Bis-Tris propane pH 7.5, 20% w/v PEG 3350 Resolution 3.90 Å R-free 0.336

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 1–1140; UniProt 1–1140 Author chain E; PDBConstruct 1–1140; UniProt 1–1140

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 C; UniProt 40–442 Not recorded Eukaryotic peptide chain release factor GTP-binding subunit ERF3A × 1 (P15170) DNA damage-binding protein 1 × 1 (Q16531) ZN ZINC ION × 1 A1IWG 2-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-6-fluoranyl-1-oxidanylidene-3~{H}-isoindole-5-carboxylic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;292 K;0.2 M Sodium citrate, 0.1 M Bis-Tris propane pH 7.5, 20% w/v PEG 3350 Resolution 3.90 Å R-free 0.336
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 40–442 Not recorded Eukaryotic peptide chain release factor GTP-binding subunit ERF3A × 1 (P15170) DNA damage-binding protein 1 × 1 (Q16531) ZN ZINC ION × 1 A1IWG 2-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-6-fluoranyl-1-oxidanylidene-3~{H}-isoindole-5-carboxylic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;292 K;0.2 M Sodium citrate, 0.1 M Bis-Tris propane pH 7.5, 20% w/v PEG 3350 Resolution 3.90 Å R-free 0.336

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 3
Chains and sequence ranges Author chain C; PDBConstruct 2–404; UniProt 40–442 Author chain F; PDBConstruct 2–404; UniProt 40–442

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 9hne

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9hne
Deposition date deposition_date2024-12-10
最后修订 last_revision2025-10-22
Structure title titleCereblon in complex with DDB1, GSPT1 and Compound-1
Keywords keywordsCRBN, GSPT1, TPD, Molecular glue, ONCOPROTEIN; ONCOPROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier62.17
Radius of gyration Rg (electron density) rg_electron63.19
Forward intensity I(0) i03833890000.00
Molecular weight molecular_weight344240.0 kDa
Excluded volume excluded_volume332830 ų
Envelope volume envelope_volume693750 ų
Hydration-shell volume shell_volume97440 ų
Envelope diameter envelope_diameter266.6
Shell Rg shell_rg58.74
Envelope Rg envelope_rg63.71
Shape Rg shape_rg63.17
Total Rg total_rg63.16
Total atoms total_atoms26021
Residues n_residues3292
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 dmax213.1
Rg (real space) rg_real62.12
Rg uncertainty (real space) rg_real_error1.95
I(0) (real space) i0_real3.8170e+09
I(0) uncertainty (real space) i0_real_error8.6550e+07
Rg (reciprocal space) rg_reciprocal61.36
I(0) (reciprocal space) i0_reciprocal3823000000.0000
Solution quality estimate total_estimate0.8409
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary68.2
Skewness Skewness skewness0.629
Kurtosis Kurtosis kurtosis0.073
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0258
Highest regularization parameter α highest_alpha109600000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.780; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.592

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)