4gpl

Structure of Cbl(TKB) bound to a phosphorylated pentapeptide

Method: X-RAY DIFFRACTION Dmax: 67.7 Å Quality: EXCELLENT

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 47–351 Fragment:human Cbl TKB domain residues 47-351 ACE-PTR-THR-PRO-GLU-PRO, PEPTIDE INHIBITOR × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.25M potassium sodium tartrate tetrahydrate, 20% w/v PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.00 Å R-free 0.248
2 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 47–351 Fragment:human Cbl TKB domain residues 47-351 ACE-PTR-THR-PRO-GLU-PRO, PEPTIDE INHIBITOR × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.25M potassium sodium tartrate tetrahydrate, 20% w/v PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.00 Å R-free 0.248

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 59 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CBL_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 5–309; UniProt 47–351

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 4gpl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4gpl
Deposition date deposition_date2012-08-21
Structure title titleStructure of Cbl(TKB) bound to a phosphorylated pentapeptide
Keywords keywordsubiquitin ligase(E3), Ligase-ligase inhibitor complex; Ligase/ligase inhibitor
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.71
Radius of gyration Rg (electron density) rg_electron20.57
Forward intensity I(0) i021053800.00
Molecular weight molecular_weight36119.0 kDa
Excluded volume excluded_volume45736 ų
Envelope volume envelope_volume53840 ų
Hydration-shell volume shell_volume21751 ų
Envelope diameter envelope_diameter67.4
Shell Rg shell_rg27.09
Envelope Rg envelope_rg20.73
Shape Rg shape_rg20.55
Total Rg total_rg21.50
Total atoms total_atoms2547
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 dmax67.7
Rg (real space) rg_real21.60
Rg uncertainty (real space) rg_real_error0.35
I(0) (real space) i0_real2.1050e+07
I(0) uncertainty (real space) i0_real_error2.6630e+05
Rg (reciprocal space) rg_reciprocal21.62
I(0) (reciprocal space) i0_reciprocal21050000.0000
Solution quality estimate total_estimate0.9052
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.2
Skewness Skewness skewness0.180
Kurtosis Kurtosis kurtosis-0.491
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8245000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.928; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd4gplb1
Class classa — All alpha proteins
Fold Fold folda.48 — N-cbl like
Superfamily Superfamily superfamilya.48.1 — N-terminal domain of cbl (N-cbl)
Family Family familya.48.1.1 — N-terminal domain of cbl (N-cbl)
Domain ID domain_idd4gplb2
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.7 — EF-hand modules in multidomain proteins
Domain ID domain_idd4gplb3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.93 — SH2-like
Superfamily Superfamily superfamilyd.93.1 — SH2 domain
Family Family familyd.93.1.1 — SH2 domain

CATH v4.4 (3 domains)

Domain ID domain_id4gplB01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology930 — Transcription Elongation Factor S-II; Chain A
Homologous superfamily homologous superfamily20 — Adaptor protein Cbl, N-terminal domain
Domain ID domain_id4gplB02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id4gplB03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology505 — SHC Adaptor Protein
Homologous superfamily homologous superfamily10 — SH2 domain

8. Citations (1)

9. Files and Curves (10)