2myl

Cullin3 - BTB interface: a novel target for stapled peptides

Method: SOLUTION NMR Dmax: 39.5 Å Quality: REASONABLE

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

Cullin-3

OrganismNot specified

UniProt Q13618

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 49–68 Fragment:UNP residues 49-68 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer SOLUTION NMR NMR measurement conditions:pH 3;298 K;Pressure ambient NMR sample composition:1 mM Cul349-68EN, trifluoroethanol/water | trifluoroethanol/water Resolution not provided

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.

29 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CUL3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–20; UniProt 49–68

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 2myl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2myl
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2myl
Deposition date deposition_date2015-01-27
Structure title titleCullin3 - BTB interface: a novel target for stapled peptides
Keywords keywordsProtein, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier9.38
Radius of gyration Rg (electron density) rg_electron9.50
Forward intensity I(0) i025365700.00
Molecular weight molecular_weight47397.0 kDa
Excluded volume excluded_volume61625 ų
Envelope volume envelope_volume5885 ų
Hydration-shell volume shell_volume5502 ų
Envelope diameter envelope_diameter38.3
Shell Rg shell_rg14.65
Envelope Rg envelope_rg11.09
Shape Rg shape_rg9.48
Total Rg total_rg9.81
Total atoms total_atoms6740
Residues n_residues360
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 dmax39.5
Rg (real space) rg_real9.71
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real2.5370e+07
I(0) uncertainty (real space) i0_real_error2.8050e+05
Rg (reciprocal space) rg_reciprocal9.70
I(0) (reciprocal space) i0_reciprocal25370000.0000
Solution quality estimate total_estimate0.6361
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary6.0
Skewness Skewness skewness0.686
Kurtosis Kurtosis kurtosis-0.258
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1786.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.089; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.001; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)