7pso

Cereblon isoform 4 from Magnetospirillum gryphiswaldense in complex with Avadomide (CC-122)

Method: X-RAY DIFFRACTION Dmax: 70.1 Å Quality: EXCELLENT

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

Cereblon isoform 4

Magnetospirillum gryphiswaldense

UniProt A4TVL0

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–124 Not recorded ZN ZINC ION × 1 EF2 S-Thalidomide × 1 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.5 M (NH4)H2PO4 Resolution 1.52 Å R-free 0.217
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–124 Not recorded ZN ZINC ION × 1 EF2 S-Thalidomide × 1 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.5 M (NH4)H2PO4 Resolution 1.52 Å R-free 0.217
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 1–124 Not recorded ZN ZINC ION × 1 PO4 PHOSPHATE ION × 1 835 (3S)-3-(5-azanyl-2-methyl-4-oxidanylidene-quinazolin-3-yl)piperidine-2,6-dione × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.5 M (NH4)H2PO4 Resolution 1.52 Å R-free 0.217

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.

61 other PDB entries and 170 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A4TVL0_9PROT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–124; UniProt 1–124 Author chain B; PDBConstruct 1–124; UniProt 1–124 Author chain C; PDBConstruct 1–124; UniProt 1–124

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 7pso

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7pso
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7pso
Deposition date deposition_date2021-09-23
Structure title titleCereblon isoform 4 from Magnetospirillum gryphiswaldense in complex with Avadomide (CC-122)
Keywords keywordsImmunomodulatory imide drug, UBIQUITIN LIGASE, PROTEIN DEGRADATION, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.44
Radius of gyration Rg (electron density) rg_electron21.52
Forward intensity I(0) i024080400.00
Molecular weight molecular_weight36439.0 kDa
Excluded volume excluded_volume44966 ų
Envelope volume envelope_volume54075 ų
Hydration-shell volume shell_volume21146 ų
Envelope diameter envelope_diameter71.0
Shell Rg shell_rg27.88
Envelope Rg envelope_rg21.44
Shape Rg shape_rg21.50
Total Rg total_rg22.40
Total atoms total_atoms2558
Residues n_residues318
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 dmax70.1
Rg (real space) rg_real22.37
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real2.4080e+07
I(0) uncertainty (real space) i0_real_error3.5870e+05
Rg (reciprocal space) rg_reciprocal22.39
I(0) (reciprocal space) i0_reciprocal24080000.0000
Solution quality estimate total_estimate0.9109
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.4
Skewness Skewness skewness0.175
Kurtosis Kurtosis kurtosis-0.576
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4236000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.947; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)