9v0b

Cryo-EM structure of avadomide-organized CRL4-DDB1-CRBN-IKZF3(ZF2-ZF3)-UbcH5a-Ub ubiquitylation assembly

Method: ELECTRON MICROSCOPY Dmax: 186.2 Å Quality: GOOD

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

Cullin-4A

Homo sapiens

UniProt Q13619

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 2–759 Not recorded DNA damage-binding protein 1 × 1 (Q16531) Protein cereblon × 1 (Q96SW2) Ubiquitin-conjugating enzyme E2 D1 × 1 (P51668) Zinc finger protein Aiolos × 1 (Q9UKT9) NEDD8 × 1 (Q15843) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 1 (P62877) Ubiquitin × 1 (P62979) ZINC ION × 6 (3S)-3-(5-azanyl-2-methyl-4-oxidanylidene-quinazolin-3-yl)piperidine-2,6-dione × 1 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.54 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CUL4A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 18–775; UniProt 2–759

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 1–1140 Not recorded Cullin-4A × 1 (Q13619) Protein cereblon × 1 (Q96SW2) Ubiquitin-conjugating enzyme E2 D1 × 1 (P51668) Zinc finger protein Aiolos × 1 (Q9UKT9) NEDD8 × 1 (Q15843) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 1 (P62877) Ubiquitin × 1 (P62979) ZINC ION × 6 (3S)-3-(5-azanyl-2-methyl-4-oxidanylidene-quinazolin-3-yl)piperidine-2,6-dione × 1 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.54 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 1–1140; UniProt 1–1140

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 41–442 Not recorded Cullin-4A × 1 (Q13619) DNA damage-binding protein 1 × 1 (Q16531) Ubiquitin-conjugating enzyme E2 D1 × 1 (P51668) Zinc finger protein Aiolos × 1 (Q9UKT9) NEDD8 × 1 (Q15843) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 1 (P62877) Ubiquitin × 1 (P62979) ZINC ION × 6 (3S)-3-(5-azanyl-2-methyl-4-oxidanylidene-quinazolin-3-yl)piperidine-2,6-dione × 1 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.54 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 3
Chains and sequence ranges Author chain C; PDBConstruct 26–427; UniProt 41–442

Ubiquitin-conjugating enzyme E2 D1

Homo sapiens

UniProt P51668

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain D; UniProt 2–147 Not recorded Cullin-4A × 1 (Q13619) DNA damage-binding protein 1 × 1 (Q16531) Protein cereblon × 1 (Q96SW2) Zinc finger protein Aiolos × 1 (Q9UKT9) NEDD8 × 1 (Q15843) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 1 (P62877) Ubiquitin × 1 (P62979) ZINC ION × 6 (3S)-3-(5-azanyl-2-methyl-4-oxidanylidene-quinazolin-3-yl)piperidine-2,6-dione × 1 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.54 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.

13 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UB2D1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–146; UniProt 2–147

Zinc finger protein Aiolos

Homo sapiens

UniProt Q9UKT9

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain I; UniProt 142–197 Not recorded Cullin-4A × 1 (Q13619) DNA damage-binding protein 1 × 1 (Q16531) Protein cereblon × 1 (Q96SW2) Ubiquitin-conjugating enzyme E2 D1 × 1 (P51668) NEDD8 × 1 (Q15843) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 1 (P62877) Ubiquitin × 1 (P62979) ZINC ION × 6 (3S)-3-(5-azanyl-2-methyl-4-oxidanylidene-quinazolin-3-yl)piperidine-2,6-dione × 1 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.54 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IKZF3_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 3–58; UniProt 142–197

NEDD8

Homo sapiens

UniProt Q15843

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain N; UniProt 1–76 Not recorded Cullin-4A × 1 (Q13619) DNA damage-binding protein 1 × 1 (Q16531) Protein cereblon × 1 (Q96SW2) Ubiquitin-conjugating enzyme E2 D1 × 1 (P51668) Zinc finger protein Aiolos × 1 (Q9UKT9) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 1 (P62877) Ubiquitin × 1 (P62979) ZINC ION × 6 (3S)-3-(5-azanyl-2-methyl-4-oxidanylidene-quinazolin-3-yl)piperidine-2,6-dione × 1 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.54 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.

46 other PDB entries and 71 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NEDD8_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain N; PDBConstruct 1–76; UniProt 1–76

E3 ubiquitin-protein ligase RBX1, N-terminally processed

Homo sapiens

UniProt P62877

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain R; UniProt 2–108 Not recorded Cullin-4A × 1 (Q13619) DNA damage-binding protein 1 × 1 (Q16531) Protein cereblon × 1 (Q96SW2) Ubiquitin-conjugating enzyme E2 D1 × 1 (P51668) Zinc finger protein Aiolos × 1 (Q9UKT9) NEDD8 × 1 (Q15843) Ubiquitin × 1 (P62979) ZINC ION × 6 (3S)-3-(5-azanyl-2-methyl-4-oxidanylidene-quinazolin-3-yl)piperidine-2,6-dione × 1 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.54 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.

99 other PDB entries and 107 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBX1_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain R; PDBConstruct 5–111; UniProt 2–108

Ubiquitin

Homo sapiens

UniProt P62979

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain U; UniProt 1–76 Not recorded Cullin-4A × 1 (Q13619) DNA damage-binding protein 1 × 1 (Q16531) Protein cereblon × 1 (Q96SW2) Ubiquitin-conjugating enzyme E2 D1 × 1 (P51668) Zinc finger protein Aiolos × 1 (Q9UKT9) NEDD8 × 1 (Q15843) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 1 (P62877) ZINC ION × 6 (3S)-3-(5-azanyl-2-methyl-4-oxidanylidene-quinazolin-3-yl)piperidine-2,6-dione × 1 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.54 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.

221 other PDB entries and 235 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS27A_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain U; PDBConstruct 1–76; UniProt 1–76

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 9v0b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9v0b
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9v0b
Deposition date deposition_date2025-05-17
Structure title titleCryo-EM structure of avadomide-organized CRL4-DDB1-CRBN-IKZF3(ZF2-ZF3)-UbcH5a-Ub ubiquitylation assembly
Keywords keywordsMolecular glue degrader, avadomide, CRL4 ubiquitin ligase, DDB1, CRBN, Complex, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.03
Radius of gyration Rg (electron density) rg_electron54.97
Forward intensity I(0) i01233110000.00
Molecular weight molecular_weight295340.0 kDa
Excluded volume excluded_volume370600 ų
Envelope volume envelope_volume592290 ų
Hydration-shell volume shell_volume90802 ų
Envelope diameter envelope_diameter185.2
Shell Rg shell_rg57.83
Envelope Rg envelope_rg52.96
Shape Rg shape_rg54.97
Total Rg total_rg55.06
Total atoms total_atoms20730
Residues n_residues2613
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 dmax186.2
Rg (real space) rg_real55.01
Rg uncertainty (real space) rg_real_error1.88
I(0) (real space) i0_real1.2330e+09
I(0) uncertainty (real space) i0_real_error2.5070e+07
Rg (reciprocal space) rg_reciprocal55.03
I(0) (reciprocal space) i0_reciprocal1233000000.0000
Solution quality estimate total_estimate0.8851
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary64.2
Skewness Skewness skewness0.250
Kurtosis Kurtosis kurtosis-0.529
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha90040000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.901; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.800

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)