9erz

Structure of CBL-TKBD bound to Ubiquitin-fused CBLock peptide

Method: X-RAY DIFFRACTION Dmax: 102.6 Å Quality: GOOD

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

E3 ubiquitin-protein ligase CBL

Homo sapiens

UniProt P22681

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 47–355 Chain C; UniProt 47–355 Not recorded Polyubiquitin-C,Ub-fused CBLock peptide × 2 (P0CG48) CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;292 K;0.1 M Bis-Tris Propane, pH 6.0, 0.2 M sodium fluoride, and 20% (v/v) PEG 3350 Resolution 2.02 Å R-free 0.229

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.

32 other PDB entries and 60 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CBL_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–311; UniProt 47–355 Author chain C; PDBConstruct 3–311; UniProt 47–355

Polyubiquitin-C,Ub-fused CBLock peptide

Homo sapiens

UniProt P0CG48

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 77–150 Chain D; UniProt 77–150 Not recorded E3 ubiquitin-protein ligase CBL × 2 (P22681) CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;292 K;0.1 M Bis-Tris Propane, pH 6.0, 0.2 M sodium fluoride, and 20% (v/v) PEG 3350 Resolution 2.02 Å R-free 0.229

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.

219 other PDB entries and 348 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBC_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 6–79; UniProt 77–150 Author chain D; PDBConstruct 6–79; UniProt 77–150

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 9erz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9erz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9erz
Deposition date deposition_date2024-03-25
Structure title titleStructure of CBL-TKBD bound to Ubiquitin-fused CBLock peptide
Keywords keywordsUbiquitin ligase, CBL, peptide inhibitor, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.61
Radius of gyration Rg (electron density) rg_electron29.74
Forward intensity I(0) i0114391000.00
Molecular weight molecular_weight85688.0 kDa
Excluded volume excluded_volume107490 ų
Envelope volume envelope_volume137790 ų
Hydration-shell volume shell_volume38840 ų
Envelope diameter envelope_diameter110.1
Shell Rg shell_rg36.79
Envelope Rg envelope_rg29.68
Shape Rg shape_rg29.74
Total Rg total_rg30.40
Total atoms total_atoms6045
Residues n_residues799
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 dmax102.6
Rg (real space) rg_real30.60
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real1.1440e+08
I(0) uncertainty (real space) i0_real_error1.8550e+06
Rg (reciprocal space) rg_reciprocal30.61
I(0) (reciprocal space) i0_reciprocal114400000.0000
Solution quality estimate total_estimate0.8760
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.5
Skewness Skewness skewness0.389
Kurtosis Kurtosis kurtosis-0.234
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha22670000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.799; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)