1yvh

Crystal Structure of the c-Cbl TKB Domain in Complex with the APS pTyr-618 Phosphopeptide

Method: X-RAY DIFFRACTION Dmax: 68.8 Å Quality: GOOD

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

CBL E3 ubiquitin protein ligase

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 A; UniProt 23–351 Fragment:Tyrosine kinase binding domain, residues 25-351 13-mer fragment of SH2 and PH domain-containing adapter protein APS × 1 (Q9Z200) MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.1;277 K;PEG 8000, magnesium acetate, sodium cacodylate, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.05 Å R-free 0.247

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 1–329; UniProt 23–351

13-mer fragment of SH2 and PH domain-containing adapter protein APS

OrganismNot specified

UniProt Q9Z200

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 609–621 Fragment:pTyr-618 phosphopeptide Non-standard monomer:Yes (specific site not provided by mmCIF) CBL E3 ubiquitin protein ligase × 1 (P22681) MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.1;277 K;PEG 8000, magnesium acetate, sodium cacodylate, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.05 Å R-free 0.247

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.

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name APS_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–13; UniProt 609–621

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 1yvh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1yvh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1yvh
Deposition date deposition_date2005-02-15
Structure title titleCrystal Structure of the c-Cbl TKB Domain in Complex with the APS pTyr-618 Phosphopeptide
Keywords keywordsX-RAY CRYSTALLOGRAPHY; PHOSPHOTYROSINE; ADAPTER PROTEIN, LIGASE, SIGNALING PROTEIN, IMMUNE SYSTEM; LIGASE,SIGNALING PROTEIN,IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.33
Radius of gyration Rg (electron density) rg_electron20.25
Forward intensity I(0) i021378900.00
Molecular weight molecular_weight36391.0 kDa
Excluded volume excluded_volume46040 ų
Envelope volume envelope_volume52832 ų
Hydration-shell volume shell_volume21641 ų
Envelope diameter envelope_diameter68.4
Shell Rg shell_rg26.77
Envelope Rg envelope_rg20.41
Shape Rg shape_rg20.24
Total Rg total_rg21.14
Total atoms total_atoms2566
Residues n_residues312
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 dmax68.8
Rg (real space) rg_real21.22
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real2.1380e+07
I(0) uncertainty (real space) i0_real_error2.7800e+05
Rg (reciprocal space) rg_reciprocal21.24
I(0) (reciprocal space) i0_reciprocal21380000.0000
Solution quality estimate total_estimate0.8958
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.3
Skewness Skewness skewness0.179
Kurtosis Kurtosis kurtosis-0.459
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6587000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.882; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1yvha1
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_idd1yvha2
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_idd1yvha3
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_id1yvhA01
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_id1yvhA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id1yvhA03
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)