9dur

Cryo-EM Structure of CRBN:dHTC1:ENL YEATS

Method: ELECTRON MICROSCOPY Dmax: 87.4 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–442 Not recorded Protein ENL × 1 (Q03111) ZN ZINC ION × 1 A1IQT 2-[3-[2-[4-[[(5~{S})-1,3-bis(oxidanylidene)-2,7-diazaspiro[4.4]nonan-7-yl]sulfonylamino]piperidin-1-yl]ethylcarbamoyl]phenyl]-~{N}-cyclobutyl-imidazo[1,2-a]pyridine-6-carboxamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;30 mM HEPES/NaOH pH7.4, 150 mM NaCl. DMSO concentrations were kept below 2% (v/v) cryo-EM vitrification conditions:Cryogen ETHANE;Grids were vitrified using a Leica EM GP plunge freezer operated at 90% humidity and 10 C. Grids were first pre-incubated with 4 uL of 10 uM CRBN-agnostic IKZF1_140-196_Q146A,G151N for 1 minute and then blotted from behind for 4 s. Immediately, 4 uL of mixturewas applied to the grids before blotting for 4 s and plunging into liquid ethane at -181 C Resolution 2.90 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 B; PDBConstruct 44–485; UniProt 1–442

Protein ENL

Homo sapiens

UniProt Q03111

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 C; UniProt 1–148 Fragment:YEATS domain Protein cereblon × 1 (Q96SW2) ZN ZINC ION × 1 A1IQT 2-[3-[2-[4-[[(5~{S})-1,3-bis(oxidanylidene)-2,7-diazaspiro[4.4]nonan-7-yl]sulfonylamino]piperidin-1-yl]ethylcarbamoyl]phenyl]-~{N}-cyclobutyl-imidazo[1,2-a]pyridine-6-carboxamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;30 mM HEPES/NaOH pH7.4, 150 mM NaCl. DMSO concentrations were kept below 2% (v/v) cryo-EM vitrification conditions:Cryogen ETHANE;Grids were vitrified using a Leica EM GP plunge freezer operated at 90% humidity and 10 C. Grids were first pre-incubated with 4 uL of 10 uM CRBN-agnostic IKZF1_140-196_Q146A,G151N for 1 minute and then blotted from behind for 4 s. Immediately, 4 uL of mixturewas applied to the grids before blotting for 4 s and plunging into liquid ethane at -181 C Resolution 2.90 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.

25 other PDB entries and 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ENL_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–148; UniProt 1–148

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 9dur

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9dur
Deposition date deposition_date2024-10-04
最后修订 last_revision2025-11-19
Structure title titleCryo-EM Structure of CRBN:dHTC1:ENL YEATS
Keywords keywordsMammalian, ENL YEATS, CRBN, dHTC1, CIP, targeted protein degradation, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier26.40
Radius of gyration Rg (electron density) rg_electron25.60
Forward intensity I(0) i054969700.00
Molecular weight molecular_weight59024.0 kDa
Excluded volume excluded_volume74336 ų
Envelope volume envelope_volume91951 ų
Hydration-shell volume shell_volume30455 ų
Envelope diameter envelope_diameter90.6
Shell Rg shell_rg32.49
Envelope Rg envelope_rg25.84
Shape Rg shape_rg25.61
Total Rg total_rg26.33
Total atoms total_atoms8268
Residues n_residues504
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 dmax87.4
Rg (real space) rg_real26.42
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real5.4970e+07
I(0) uncertainty (real space) i0_real_error8.2150e+05
Rg (reciprocal space) rg_reciprocal26.41
I(0) (reciprocal space) i0_reciprocal54970000.0000
Solution quality estimate total_estimate0.8755
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.1
Skewness Skewness skewness0.447
Kurtosis Kurtosis kurtosis-0.049
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15820000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.808; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.964

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)