5oh1

Cereblon isoform 4 from Magnetospirillum gryphiswaldense in complex with Aminoglutethimide

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 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;0.1 M sodium acetate PH 4.6, 15 %(W/V) PEG 20000 Resolution 1.70 Å R-free 0.210
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 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;0.1 M sodium acetate PH 4.6, 15 %(W/V) PEG 20000 Resolution 1.70 Å R-free 0.210
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 9UQ (3~{R})-3-(4-aminophenyl)-3-ethyl-piperidine-2,6-dione × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;0.1 M sodium acetate PH 4.6, 15 %(W/V) PEG 20000 Resolution 1.70 Å R-free 0.210

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 2–125; UniProt 1–124 Author chain B; PDBConstruct 2–125; UniProt 1–124 Author chain C; 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 5oh1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5oh1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5oh1
Deposition date deposition_date2017-07-14
Structure title titleCereblon isoform 4 from Magnetospirillum gryphiswaldense in complex with Aminoglutethimide
Keywords keywordsTeratogenicity, Protein degradation, Substrate recognition, Ubiquitin ligase, UNKNOWN FUNCTION; UNKNOWN FUNCTION
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) i021907500.00
Molecular weight molecular_weight35379.0 kDa
Excluded volume excluded_volume43975 ų
Envelope volume envelope_volume52688 ų
Hydration-shell volume shell_volume20707 ų
Envelope diameter envelope_diameter71.1
Shell Rg shell_rg27.73
Envelope Rg envelope_rg21.40
Shape Rg shape_rg21.50
Total Rg total_rg22.39
Total atoms total_atoms2489
Residues n_residues309
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_error0.35
I(0) (real space) i0_real2.1910e+07
I(0) uncertainty (real space) i0_real_error2.7690e+05
Rg (reciprocal space) rg_reciprocal22.39
I(0) (reciprocal space) i0_reciprocal21910000.0000
Solution quality estimate total_estimate0.9118
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.4
Skewness Skewness skewness0.168
Kurtosis Kurtosis kurtosis-0.594
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3235000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.986

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)