9dqd

cryo-EM structure of human Cereblon/DDB1 in complex with a non-traditional CRBN binder

Method: ELECTRON MICROSCOPY Dmax: 109.9 Å Quality: EXCELLENT

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–442 Not recorded DNA damage-binding protein 1 × 1 (Q16531) ZN ZINC ION × 1 A1BEP (3R)-3-{1-methyl-6-[(piperidin-4-yl)amino]-1H-indazol-3-yl}piperidine-2,6-dione × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

93 other PDB entries and 141 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 26–467; UniProt 1–442

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–395 Chain B; UniProt 706–1140 Mutation:deletion of residues 396-705 Protein cereblon × 1 (Q96SW2) ZN ZINC ION × 1 A1BEP (3R)-3-{1-methyl-6-[(piperidin-4-yl)amino]-1H-indazol-3-yl}piperidine-2,6-dione × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

202 other PDB entries and 290 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

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 9dqd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9dqd
Deposition date deposition_date2024-09-23
Structure title titlecryo-EM structure of human Cereblon/DDB1 in complex with a non-traditional CRBN binder
Keywords keywordsCRL4, UBIQUITIN, E3, CEREBLON, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.85
Radius of gyration Rg (electron density) rg_electron34.26
Forward intensity I(0) i0530378000.00
Molecular weight molecular_weight124180.0 kDa
Excluded volume excluded_volume120120 ų
Envelope volume envelope_volume218280 ų
Hydration-shell volume shell_volume52461 ų
Envelope diameter envelope_diameter111.7
Shell Rg shell_rg41.48
Envelope Rg envelope_rg33.82
Shape Rg shape_rg34.30
Total Rg total_rg34.58
Total atoms total_atoms9409
Residues n_residues1181
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 dmax109.9
Rg (real space) rg_real34.73
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real5.3040e+08
I(0) uncertainty (real space) i0_real_error8.8370e+06
Rg (reciprocal space) rg_reciprocal34.81
I(0) (reciprocal space) i0_reciprocal530400000.0000
Solution quality estimate total_estimate0.9003
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.5
Skewness Skewness skewness0.204
Kurtosis Kurtosis kurtosis-0.528
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha59710000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.931; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.912

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)