6r1d

Cereblon isoform 4 from Magnetospirillum gryphiswaldense in complex with compound 7d, co-crystallized

Method: X-RAY DIFFRACTION Dmax: 62.5 Å Quality: GOOD

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

Cereblon isoform 4

Magnetospirillum gryphiswaldense MSR-1

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 JP5 (phenylmethyl) ~{N}-[(3~{S})-2,5-bis(oxidanylidene)pyrrolidin-3-yl]carbamate × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;15 % PEG 6K, 5 % Glycerol Resolution 1.10 Å R-free 0.150
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 JP5 (phenylmethyl) ~{N}-[(3~{S})-2,5-bis(oxidanylidene)pyrrolidin-3-yl]carbamate × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;15 % PEG 6K, 5 % Glycerol Resolution 1.10 Å R-free 0.150

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 171 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 2–125; UniProt 1–124 Author chain B; PDBConstruct 2–125; 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 6r1d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6r1d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6r1d
Deposition date deposition_date2019-03-14
Structure title titleCereblon isoform 4 from Magnetospirillum gryphiswaldense in complex with compound 7d, co-crystallized
Keywords keywordsproteolysis targeting chimera, PROTAC, 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_guinier19.66
Radius of gyration Rg (electron density) rg_electron18.77
Forward intensity I(0) i010890500.00
Molecular weight molecular_weight24199.0 kDa
Excluded volume excluded_volume29962 ų
Envelope volume envelope_volume34521 ų
Hydration-shell volume shell_volume16020 ų
Envelope diameter envelope_diameter62.0
Shell Rg shell_rg24.14
Envelope Rg envelope_rg18.86
Shape Rg shape_rg18.68
Total Rg total_rg19.81
Total atoms total_atoms1701
Residues n_residues211
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 dmax62.5
Rg (real space) rg_real19.65
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real1.0890e+07
I(0) uncertainty (real space) i0_real_error1.3490e+05
Rg (reciprocal space) rg_reciprocal19.65
I(0) (reciprocal space) i0_reciprocal10890000.0000
Solution quality estimate total_estimate0.8985
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.0
Skewness Skewness skewness0.282
Kurtosis Kurtosis kurtosis-0.549
Angular range angular_range— – 0.4050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1530000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.922; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.935

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)