4v31

Cereblon isoform 4 from Magnetospirillum gryphiswaldense in complex with Deoxyuridine

Method: X-RAY DIFFRACTION Dmax: 68.7 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 DUR 2'-DEOXYURIDINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:0.1 M CITRIC ACID PH 3.5, 25 %(W/V) PEG 3350 Resolution 1.80 Å R-free 0.219
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 DUR 2'-DEOXYURIDINE × 1 FLC CITRATE ANION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:0.1 M CITRIC ACID PH 3.5, 25 %(W/V) PEG 3350 Resolution 1.80 Å R-free 0.219
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 DUR 2'-DEOXYURIDINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:0.1 M CITRIC ACID PH 3.5, 25 %(W/V) PEG 3350 Resolution 1.80 Å R-free 0.219

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 4v31

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4v31
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4v31
Deposition date deposition_date2014-10-15
Structure title titleCereblon isoform 4 from Magnetospirillum gryphiswaldense in complex with Deoxyuridine
Keywords keywordsSIGNALING PROTEIN, TERATOGENICITY, AROMATIC CAGE; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.37
Radius of gyration Rg (electron density) rg_electron21.46
Forward intensity I(0) i023642800.00
Molecular weight molecular_weight36493.0 kDa
Excluded volume excluded_volume45219 ų
Envelope volume envelope_volume54194 ų
Hydration-shell volume shell_volume21258 ų
Envelope diameter envelope_diameter70.2
Shell Rg shell_rg27.79
Envelope Rg envelope_rg21.36
Shape Rg shape_rg21.43
Total Rg total_rg22.35
Total atoms total_atoms2566
Residues n_residues323
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 dmax68.7
Rg (real space) rg_real22.29
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real2.3640e+07
I(0) uncertainty (real space) i0_real_error2.9520e+05
Rg (reciprocal space) rg_reciprocal22.31
I(0) (reciprocal space) i0_reciprocal23640000.0000
Solution quality estimate total_estimate0.9139
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.9
Skewness Skewness skewness0.168
Kurtosis Kurtosis kurtosis-0.591
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3454000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.963; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id4v31A00
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology150 — Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A
Homologous superfamily homologous superfamily20 — Peptide methionine sulfoxide reductase.
Domain ID domain_id4v31B00
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology150 — Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A
Homologous superfamily homologous superfamily20 — Peptide methionine sulfoxide reductase.
Domain ID domain_id4v31C00
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology150 — Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A
Homologous superfamily homologous superfamily20 — Peptide methionine sulfoxide reductase.

8. Citations (1)

9. Files and Curves (10)