7pjk

Cereblon isoform 4 from Magnetospirillum gryphiswaldense in complex with a benzotriazole analog of thalidomide

Method: X-RAY DIFFRACTION Dmax: 64.5 Å Quality: EXCELLENT

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 7SE (3S)-3-(benzotriazol-2-yl)piperidine-2,6-dione × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.4 M (NH4)2HPO4 Resolution 1.99 Å R-free 0.254
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 7SE (3S)-3-(benzotriazol-2-yl)piperidine-2,6-dione × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.4 M (NH4)2HPO4 Resolution 1.99 Å R-free 0.254
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 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.4 M (NH4)2HPO4 Resolution 1.99 Å R-free 0.254

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 7pjk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7pjk
Deposition date deposition_date2021-08-24
Structure title titleCereblon isoform 4 from Magnetospirillum gryphiswaldense in complex with a benzotriazole analog of thalidomide
Keywords keywordsSIGNALING PROTEIN, THALIDOMIDE ANALOGUES; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.99
Radius of gyration Rg (electron density) rg_electron20.20
Forward intensity I(0) i016151100.00
Molecular weight molecular_weight29877.0 kDa
Excluded volume excluded_volume37069 ų
Envelope volume envelope_volume44628 ų
Hydration-shell volume shell_volume18751 ų
Envelope diameter envelope_diameter65.6
Shell Rg shell_rg25.95
Envelope Rg envelope_rg20.23
Shape Rg shape_rg20.17
Total Rg total_rg21.08
Total atoms total_atoms2096
Residues n_residues265
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 dmax64.5
Rg (real space) rg_real20.91
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real1.6150e+07
I(0) uncertainty (real space) i0_real_error2.0840e+05
Rg (reciprocal space) rg_reciprocal20.92
I(0) (reciprocal space) i0_reciprocal16150000.0000
Solution quality estimate total_estimate0.9157
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.3
Skewness Skewness skewness0.163
Kurtosis Kurtosis kurtosis-0.584
Angular range angular_range— – 0.3800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2311000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.968; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)