Crystal structure of c-Cbl TKB domain in complex with double phosphorylated Spry2 peptide. Determined by X-ray diffraction at 2.2 Å resolution. Released 18 Aug 2010.
Explore 3OB1 in 3D Show helices and sheets RCSB PDB PDBe
3OB1 contains 17 α-helices and 7 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 56-70 | 15 | |
| α-helix | 73-75 | 3 | |
| α-helix | 84-101 | 18 | |
| α-helix | 106-111 | 6 | |
| α-helix | 113-136 | 24 | |
| α-helix | 137-141 | 5 | |
| α-helix | 146-168 | 23 | |
| α-helix | 170-172 | 3 | |
| α-helix | 184-194 | 11 | |
| β-strand | 199-201 | 3 | 1 |
| α-helix | 202-212 | 11 | |
| α-helix | 218-228 | 11 | |
| β-strand | 235-237 | 3 | 1 |
| α-helix | 238-247 | 10 | |
| α-helix | 251-253 | 3 | |
| α-helix | 254-258 | 5 | |
| α-helix | 259-263 | 5 | |
| β-strand | 268 | 1 | 2 |
| α-helix | 274-282 | 9 | |
| β-strand | 290-295 | 6 | 2 |
| β-strand | 303-308 | 6 | 2 |
| β-strand | 314-317 | 4 | 2 |
| α-helix | 324-333 | 10 | |
| β-strand | 339-340 | 2 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 12-meric peptide from Protein sprouty homolog 2 | A | protein | 12 | Homo sapiens | O43597 (AlphaFold model) |
| E3 ubiquitin-protein ligase CBL | B | protein | 329 | Homo sapiens | P22681 (AlphaFold model) |
>3OB1_1 12-meric peptide from Protein sprouty homolog 2 (chains A) IRNTNEYTEGPT
>3OB1_2 E3 ubiquitin-protein ligase CBL (chains B) GSLIGLMKDAFQPHHHHHHHLSPHPPGTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPP YILDLLPDTYQHLRTILSRYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYE ENSQPRRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVPW KSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWSSLLRNWNSLA VTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLSCTRLGQWAIGYVTADGNILQTIPHNK PLFQALIDGFREGFYLFPDGRNQNPDLTG
Additional serine/threonine phosphorylation reduces binding affinity but preserves interface topography of substrate proteins to the c-Cbl TKB domain. Sun, Q., Jackson, R.A., Ng, C. et al. PLoS One (2010) 5:e12819-e12819. DOI 10.1371/journal.pone.0012819 · PubMed
Other PDB entries of the same protein (UniProt O43597 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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