9e2u

Crystal structure of DDB1-CRBN-ALV1 complex bound to triple ZnF of Helios (IKZF2 ZF1-3)

Method: X-RAY DIFFRACTION Dmax: 214.5 Å Quality: EXCELLENT

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 I; UniProt 1–395 Chain I; UniProt 706–1140 Fragment:internal deletion of the BPB domain,internal deletion of the BPB domain Protein cereblon × 1 (Q96SW2) Zinc finger protein Helios × 1 RN9 3-[3-[[1-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-2,5-bis(oxidanylidene)pyrrol-3-yl]amino]phenyl]-~{N}-(3-chloranyl-4-methyl-phenyl)propanamide × 1 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20.455% PEG 3350, 0.214 M Li3 Cit Resolution 4.11 Å R-free 0.289
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–395 Chain A; UniProt 706–1140 Fragment:internal deletion of the BPB domain,internal deletion of the BPB domain Protein cereblon × 1 (Q96SW2) Zinc finger protein Helios × 1 RN9 3-[3-[[1-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-2,5-bis(oxidanylidene)pyrrol-3-yl]amino]phenyl]-~{N}-(3-chloranyl-4-methyl-phenyl)propanamide × 1 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20.455% PEG 3350, 0.214 M Li3 Cit Resolution 4.11 Å R-free 0.289
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–395 Chain C; UniProt 706–1140 Fragment:internal deletion of the BPB domain,internal deletion of the BPB domain Protein cereblon × 1 (Q96SW2) Zinc finger protein Helios × 1 RN9 3-[3-[[1-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-2,5-bis(oxidanylidene)pyrrol-3-yl]amino]phenyl]-~{N}-(3-chloranyl-4-methyl-phenyl)propanamide × 1 ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20.455% PEG 3350, 0.214 M Li3 Cit Resolution 4.11 Å R-free 0.289
4 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 1–395 Chain E; UniProt 706–1140 Fragment:internal deletion of the BPB domain,internal deletion of the BPB domain Protein cereblon × 1 (Q96SW2) Zinc finger protein Helios × 1 RN9 3-[3-[[1-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-2,5-bis(oxidanylidene)pyrrol-3-yl]amino]phenyl]-~{N}-(3-chloranyl-4-methyl-phenyl)propanamide × 1 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20.455% PEG 3350, 0.214 M Li3 Cit Resolution 4.11 Å R-free 0.289
5 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain G; UniProt 1–395 Chain G; UniProt 706–1140 Fragment:internal deletion of the BPB domain,internal deletion of the BPB domain Protein cereblon × 1 (Q96SW2) Zinc finger protein Helios × 1 RN9 3-[3-[[1-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-2,5-bis(oxidanylidene)pyrrol-3-yl]amino]phenyl]-~{N}-(3-chloranyl-4-methyl-phenyl)propanamide × 1 ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20.455% PEG 3350, 0.214 M Li3 Cit Resolution 4.11 Å R-free 0.289
6 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain K; UniProt 1–395 Chain K; UniProt 706–1140 Fragment:internal deletion of the BPB domain,internal deletion of the BPB domain Protein cereblon × 1 (Q96SW2) Zinc finger protein Helios × 1 RN9 3-[3-[[1-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-2,5-bis(oxidanylidene)pyrrol-3-yl]amino]phenyl]-~{N}-(3-chloranyl-4-methyl-phenyl)propanamide × 1 ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20.455% PEG 3350, 0.214 M Li3 Cit Resolution 4.11 Å R-free 0.289
7 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain M; UniProt 1–395 Chain M; UniProt 706–1140 Fragment:internal deletion of the BPB domain,internal deletion of the BPB domain Protein cereblon × 1 (Q96SW2) Zinc finger protein Helios × 1 RN9 3-[3-[[1-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-2,5-bis(oxidanylidene)pyrrol-3-yl]amino]phenyl]-~{N}-(3-chloranyl-4-methyl-phenyl)propanamide × 1 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20.455% PEG 3350, 0.214 M Li3 Cit Resolution 4.11 Å R-free 0.289
8 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain O; UniProt 1–395 Chain O; UniProt 706–1140 Fragment:internal deletion of the BPB domain,internal deletion of the BPB domain Protein cereblon × 1 (Q96SW2) Zinc finger protein Helios × 1 RN9 3-[3-[[1-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-2,5-bis(oxidanylidene)pyrrol-3-yl]amino]phenyl]-~{N}-(3-chloranyl-4-methyl-phenyl)propanamide × 1 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20.455% PEG 3350, 0.214 M Li3 Cit Resolution 4.11 Å R-free 0.289

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 283 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 29–423; UniProt 1–395 Author chain A; PDBConstruct 430–864; UniProt 706–1140 Author chain C; PDBConstruct 29–423; UniProt 1–395 Author chain C; PDBConstruct 430–864; UniProt 706–1140 Author chain E; PDBConstruct 29–423; UniProt 1–395 Author chain E; PDBConstruct 430–864; UniProt 706–1140 Author chain G; PDBConstruct 29–423; UniProt 1–395 Author chain G; PDBConstruct 430–864; UniProt 706–1140 Author chain I; PDBConstruct 29–423; UniProt 1–395 Author chain I; PDBConstruct 430–864; UniProt 706–1140 Author chain K; PDBConstruct 29–423; UniProt 1–395 Author chain K; PDBConstruct 430–864; UniProt 706–1140 Author chain M; PDBConstruct 29–423; UniProt 1–395 Author chain M; PDBConstruct 430–864; UniProt 706–1140 Author chain O; PDBConstruct 29–423; UniProt 1–395 Author chain O; PDBConstruct 430–864; UniProt 706–1140

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 J; UniProt 1–441 Not recorded DNA damage-binding protein 1 × 1 (Q16531) Zinc finger protein Helios × 1 RN9 3-[3-[[1-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-2,5-bis(oxidanylidene)pyrrol-3-yl]amino]phenyl]-~{N}-(3-chloranyl-4-methyl-phenyl)propanamide × 1 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20.455% PEG 3350, 0.214 M Li3 Cit Resolution 4.11 Å R-free 0.289
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–441 Not recorded DNA damage-binding protein 1 × 1 (Q16531) Zinc finger protein Helios × 1 RN9 3-[3-[[1-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-2,5-bis(oxidanylidene)pyrrol-3-yl]amino]phenyl]-~{N}-(3-chloranyl-4-methyl-phenyl)propanamide × 1 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20.455% PEG 3350, 0.214 M Li3 Cit Resolution 4.11 Å R-free 0.289
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 1–441 Not recorded DNA damage-binding protein 1 × 1 (Q16531) Zinc finger protein Helios × 1 RN9 3-[3-[[1-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-2,5-bis(oxidanylidene)pyrrol-3-yl]amino]phenyl]-~{N}-(3-chloranyl-4-methyl-phenyl)propanamide × 1 ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20.455% PEG 3350, 0.214 M Li3 Cit Resolution 4.11 Å R-free 0.289
4 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 1–441 Not recorded DNA damage-binding protein 1 × 1 (Q16531) Zinc finger protein Helios × 1 RN9 3-[3-[[1-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-2,5-bis(oxidanylidene)pyrrol-3-yl]amino]phenyl]-~{N}-(3-chloranyl-4-methyl-phenyl)propanamide × 1 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20.455% PEG 3350, 0.214 M Li3 Cit Resolution 4.11 Å R-free 0.289
5 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain H; UniProt 1–441 Not recorded DNA damage-binding protein 1 × 1 (Q16531) Zinc finger protein Helios × 1 RN9 3-[3-[[1-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-2,5-bis(oxidanylidene)pyrrol-3-yl]amino]phenyl]-~{N}-(3-chloranyl-4-methyl-phenyl)propanamide × 1 ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20.455% PEG 3350, 0.214 M Li3 Cit Resolution 4.11 Å R-free 0.289
6 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain L; UniProt 1–441 Not recorded DNA damage-binding protein 1 × 1 (Q16531) Zinc finger protein Helios × 1 RN9 3-[3-[[1-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-2,5-bis(oxidanylidene)pyrrol-3-yl]amino]phenyl]-~{N}-(3-chloranyl-4-methyl-phenyl)propanamide × 1 ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20.455% PEG 3350, 0.214 M Li3 Cit Resolution 4.11 Å R-free 0.289
7 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain N; UniProt 1–441 Not recorded DNA damage-binding protein 1 × 1 (Q16531) Zinc finger protein Helios × 1 RN9 3-[3-[[1-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-2,5-bis(oxidanylidene)pyrrol-3-yl]amino]phenyl]-~{N}-(3-chloranyl-4-methyl-phenyl)propanamide × 1 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20.455% PEG 3350, 0.214 M Li3 Cit Resolution 4.11 Å R-free 0.289
8 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain P; UniProt 1–441 Not recorded DNA damage-binding protein 1 × 1 (Q16531) Zinc finger protein Helios × 1 RN9 3-[3-[[1-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-2,5-bis(oxidanylidene)pyrrol-3-yl]amino]phenyl]-~{N}-(3-chloranyl-4-methyl-phenyl)propanamide × 1 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20.455% PEG 3350, 0.214 M Li3 Cit Resolution 4.11 Å R-free 0.289

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 134 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CRBN_HUMAN
Isoform Q96SW2-2
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 23–463; UniProt 1–441 Author chain D; PDBConstruct 23–463; UniProt 1–441 Author chain F; PDBConstruct 23–463; UniProt 1–441 Author chain H; PDBConstruct 23–463; UniProt 1–441 Author chain J; PDBConstruct 23–463; UniProt 1–441 Author chain L; PDBConstruct 23–463; UniProt 1–441 Author chain N; PDBConstruct 23–463; UniProt 1–441 Author chain P; PDBConstruct 23–463; UniProt 1–441

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 9e2u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9e2u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9e2u
Deposition date deposition_date2024-10-23
最后修订 last_revision2025-09-03
Structure title titleCrystal structure of DDB1-CRBN-ALV1 complex bound to triple ZnF of Helios (IKZF2 ZF1-3)
Keywords keywordsCRBN, DDB1, IKZF2, ALV1, DEGRADATION, E3 LIGASE, LIGASE, MOLECULAR GLUE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier84.99
Radius of gyration Rg (electron density) rg_electron84.40
Forward intensity I(0) i018676900000.00
Molecular weight molecular_weight1163800.0 kDa
Excluded volume excluded_volume1455800 ų
Envelope volume envelope_volume2408700 ų
Hydration-shell volume shell_volume235560 ų
Envelope diameter envelope_diameter297.1
Shell Rg shell_rg84.02
Envelope Rg envelope_rg81.84
Shape Rg shape_rg84.35
Total Rg total_rg84.59
Total atoms total_atoms81784
Residues n_residues10322
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 dmax214.5
Rg (real space) rg_real82.09
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real1.7920e+10
I(0) uncertainty (real space) i0_real_error3.1030e+08
Rg (reciprocal space) rg_reciprocal85.71
I(0) (reciprocal space) i0_reciprocal18720000000.0000
Solution quality estimate total_estimate0.9087
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary107.2
Skewness Skewness skewness0.090
Kurtosis Kurtosis kurtosis-0.557
Angular range angular_range— – 0.0900 −1
Current regularization parameter α current_alpha0.6512
Highest regularization parameter α highest_alpha477100000.0000
Real-space data points n_real_points19
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 1.000; Stabil: 0.979; Sysdev: 1.000; Positv: 1.000; Valcen: 0.876; Smooth: 0.001

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (2)

9. Files and Curves (10)