7bqv

Cereblon in complex with SALL4 and (S)-5-hydroxythalidomide

Method: X-RAY DIFFRACTION Dmax: 50.0 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 A; UniProt 318–426 Mutation:C366S Sal-like protein 4 × 1 (Q9UJQ4) F4U 2-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-5-oxidanyl-isoindole-1,3-dione × 1 ZN ZINC ION × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;22% PEG 4000, 0.1 M MES (pH 6.0), 0.2 M lithium sulfate Resolution 1.80 Å R-free 0.223

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 A; PDBConstruct 1–109; UniProt 318–426

Sal-like protein 4

Homo sapiens

UniProt Q9UJQ4

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 410–432 Not recorded Protein cereblon × 1 (Q96SW2) F4U 2-[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]-5-oxidanyl-isoindole-1,3-dione × 1 ZN ZINC ION × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;22% PEG 4000, 0.1 M MES (pH 6.0), 0.2 M lithium sulfate Resolution 1.80 Å R-free 0.223

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.

11 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SALL4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–24; UniProt 410–432

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 7bqv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7bqv
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7bqv
Deposition date deposition_date2020-03-25
Structure title titleCereblon in complex with SALL4 and (S)-5-hydroxythalidomide
Keywords keywordsZINC FINGER, E3 UBIQUITIN LIGASE, COMPLEX, THALIDOMIDE, METAL BINDING PROTEIN; METAL BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.50
Radius of gyration Rg (electron density) rg_electron14.41
Forward intensity I(0) i05056970.00
Molecular weight molecular_weight15593.0 kDa
Excluded volume excluded_volume19252 ų
Envelope volume envelope_volume21589 ų
Hydration-shell volume shell_volume12753 ų
Envelope diameter envelope_diameter48.3
Shell Rg shell_rg20.20
Envelope Rg envelope_rg14.79
Shape Rg shape_rg14.35
Total Rg total_rg15.71
Total atoms total_atoms1083
Residues n_residues133
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 dmax50.0
Rg (real space) rg_real15.42
Rg uncertainty (real space) rg_real_error0.25
I(0) (real space) i0_real5.0570e+06
I(0) uncertainty (real space) i0_real_error5.4170e+04
Rg (reciprocal space) rg_reciprocal15.43
I(0) (reciprocal space) i0_reciprocal5057000.0000
Solution quality estimate total_estimate0.8908
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary49.4
Skewness Skewness skewness0.175
Kurtosis Kurtosis kurtosis-0.364
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha782900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.866; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.977

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)