8dey

Ternary complex structure of Cereblon-DDB1 bound to IKZF2(ZF2,3) and the molecular glue DKY709

Method: X-RAY DIFFRACTION Dmax: 199.7 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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 70–442 Not recorded DNA damage-binding protein 1 × 1 (Q16531) Zinc finger protein Helios × 1 (Q9UKS7) ZN ZINC ION × 3 LWK (3S)-3-[5-(1-benzylpiperidin-4-yl)-1-oxo-1,3-dihydro-2H-isoindol-2-yl]piperidine-2,6-dione × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;1.6 M potassium/sodium phosphate, pH 6.5 Resolution 3.70 Å R-free 0.348
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 70–442 Not recorded DNA damage-binding protein 1 × 1 (Q16531) Zinc finger protein Helios × 1 (Q9UKS7) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;1.6 M potassium/sodium phosphate, pH 6.5 Resolution 3.70 Å R-free 0.348

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–373; UniProt 70–442 Author chain D; PDBConstruct 1–373; UniProt 70–442

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–395 Chain B; UniProt 706–1140 Fragment:UNP residues 1-395,706-1140,UNP residues 1-395,706-1140 Protein cereblon × 1 (Q96SW2) Zinc finger protein Helios × 1 (Q9UKS7) ZN ZINC ION × 3 LWK (3S)-3-[5-(1-benzylpiperidin-4-yl)-1-oxo-1,3-dihydro-2H-isoindol-2-yl]piperidine-2,6-dione × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;1.6 M potassium/sodium phosphate, pH 6.5 Resolution 3.70 Å R-free 0.348
2 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:UNP residues 1-395,706-1140,UNP residues 1-395,706-1140 Protein cereblon × 1 (Q96SW2) Zinc finger protein Helios × 1 (Q9UKS7) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;1.6 M potassium/sodium phosphate, pH 6.5 Resolution 3.70 Å R-free 0.348

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 1–395; UniProt 1–395 Author chain B; PDBConstruct 402–836; UniProt 706–1140 Author chain E; PDBConstruct 1–395; UniProt 1–395 Author chain E; PDBConstruct 402–836; UniProt 706–1140

Zinc finger protein Helios

Homo sapiens

UniProt Q9UKS7

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 137–192 Fragment:IKZF2 (UNP residues 137-192) Protein cereblon × 1 (Q96SW2) DNA damage-binding protein 1 × 1 (Q16531) ZN ZINC ION × 3 LWK (3S)-3-[5-(1-benzylpiperidin-4-yl)-1-oxo-1,3-dihydro-2H-isoindol-2-yl]piperidine-2,6-dione × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;1.6 M potassium/sodium phosphate, pH 6.5 Resolution 3.70 Å R-free 0.348
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 137–192 Fragment:IKZF2 (UNP residues 137-192) Protein cereblon × 1 (Q96SW2) DNA damage-binding protein 1 × 1 (Q16531) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;1.6 M potassium/sodium phosphate, pH 6.5 Resolution 3.70 Å R-free 0.348

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 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IKZF2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 2–57; UniProt 137–192 Author chain F; PDBConstruct 2–57; UniProt 137–192

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 8dey

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8dey
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8dey
Deposition date deposition_date2022-06-21
Structure title titleTernary complex structure of Cereblon-DDB1 bound to IKZF2(ZF2,3) and the molecular glue DKY709
Keywords keywordsE3 ligase, molecular glue, complex, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier56.67
Radius of gyration Rg (electron density) rg_electron57.03
Forward intensity I(0) i01075630000.00
Molecular weight molecular_weight275410.0 kDa
Excluded volume excluded_volume345090 ų
Envelope volume envelope_volume512010 ų
Hydration-shell volume shell_volume77343 ų
Envelope diameter envelope_diameter217.2
Shell Rg shell_rg56.65
Envelope Rg envelope_rg56.52
Shape Rg shape_rg57.01
Total Rg total_rg57.06
Total atoms total_atoms19332
Residues n_residues2460
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 dmax199.7
Rg (real space) rg_real57.32
Rg uncertainty (real space) rg_real_error2.66
I(0) (real space) i0_real1.0760e+09
I(0) uncertainty (real space) i0_real_error2.4220e+07
Rg (reciprocal space) rg_reciprocal56.13
I(0) (reciprocal space) i0_reciprocal1074000000.0000
Solution quality estimate total_estimate0.7900
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.9
Skewness Skewness skewness0.617
Kurtosis Kurtosis kurtosis-0.147
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha125900000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.664; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.804; Smooth: 0.471

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

Domain ID domain_id8deyA01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology130 — Archaeosine Trna-guanine Transglycosylase; Chain: A, domain 4
Homologous superfamily homologous superfamily40 — LON domain-like
Domain ID domain_id8deyA02
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology150 — Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A
Homologous superfamily homologous superfamily20 — Peptide methionine sulfoxide reductase.
Domain ID domain_id8deyB01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id8deyB02
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id8deyB03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily910
Domain ID domain_id8deyD01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology130 — Archaeosine Trna-guanine Transglycosylase; Chain: A, domain 4
Homologous superfamily homologous superfamily40 — LON domain-like
Domain ID domain_id8deyD02
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology150 — Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A
Homologous superfamily homologous superfamily20 — Peptide methionine sulfoxide reductase.
Domain ID domain_id8deyE01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id8deyE02
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id8deyE03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily910

8. Citations (1)

9. Files and Curves (10)