9oty

DDB1-CRBN with CK1 alpha, SB-405483, and DEG-47: composite map and model submission

Method: ELECTRON MICROSCOPY Dmax: 152.7 Å Quality: GOOD

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

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 A; UniProt 1–391 Chain A; UniProt 710–1140 Not recorded Protein cereblon × 1 (Q96SW2) Casein kinase I isoform alpha × 1 (P48729) ZN ZINC ION × 1 A1CEH N-{2-[(3R)-2,6-dioxopiperidin-3-yl]-1-oxo-2,3-dihydro-1H-isoindol-5-yl}benzamide × 1 A1CEG N-[3-(benzyloxy)pyridin-2-yl]-N'-(4-cyano-2-hydroxyphenyl)urea × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;10mM HEPES, 240mM NaCl, 3mM TCEP 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–391; UniProt 1–391 Author chain A; PDBConstruct 392–822; UniProt 710–1140

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 B; UniProt 46–427 Not recorded DNA damage-binding protein 1 × 1 (Q16531) Casein kinase I isoform alpha × 1 (P48729) ZN ZINC ION × 1 A1CEH N-{2-[(3R)-2,6-dioxopiperidin-3-yl]-1-oxo-2,3-dihydro-1H-isoindol-5-yl}benzamide × 1 A1CEG N-[3-(benzyloxy)pyridin-2-yl]-N'-(4-cyano-2-hydroxyphenyl)urea × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;10mM HEPES, 240mM NaCl, 3mM TCEP 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–382; UniProt 46–427

Casein kinase I isoform alpha

Homo sapiens

UniProt P48729

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 10–303 Not recorded DNA damage-binding protein 1 × 1 (Q16531) Protein cereblon × 1 (Q96SW2) ZN ZINC ION × 1 A1CEH N-{2-[(3R)-2,6-dioxopiperidin-3-yl]-1-oxo-2,3-dihydro-1H-isoindol-5-yl}benzamide × 1 A1CEG N-[3-(benzyloxy)pyridin-2-yl]-N'-(4-cyano-2-hydroxyphenyl)urea × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;10mM HEPES, 240mM NaCl, 3mM TCEP 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.

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

View Construct and Data Evidence
UniProt name KC1A_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–294; UniProt 10–303

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 9oty

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9oty
Deposition date deposition_date2025-05-27
Structure title titleDDB1-CRBN with CK1 alpha, SB-405483, and DEG-47: composite map and model submission
Keywords keywordsE3 ligases, Cullin RING Ligase, CRL4, Cereblon, CRBN, molecular glues, IMiDs, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.29
Radius of gyration Rg (electron density) rg_electron43.58
Forward intensity I(0) i0777588000.00
Molecular weight molecular_weight152560.0 kDa
Excluded volume excluded_volume147740 ų
Envelope volume envelope_volume292280 ų
Hydration-shell volume shell_volume58155 ų
Envelope diameter envelope_diameter155.0
Shell Rg shell_rg45.62
Envelope Rg envelope_rg44.29
Shape Rg shape_rg43.58
Total Rg total_rg43.65
Total atoms total_atoms11542
Residues n_residues1438
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 dmax152.7
Rg (real space) rg_real43.71
Rg uncertainty (real space) rg_real_error1.44
I(0) (real space) i0_real7.7760e+08
I(0) uncertainty (real space) i0_real_error1.5110e+07
Rg (reciprocal space) rg_reciprocal43.30
I(0) (reciprocal space) i0_reciprocal777200000.0000
Solution quality estimate total_estimate0.8068
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.4
Skewness Skewness skewness0.609
Kurtosis Kurtosis kurtosis-0.181
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha100300000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.678; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.806; Smooth: 0.644

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)