Structure of c-Cbl-ZAP-70 peptide complex. Determined by X-ray diffraction at 2.0 Å resolution. Released 18 Jan 2012.
Explore 2Y1N in 3D Show helices and sheets RCSB PDB PDBe
2Y1N contains 47 α-helices and 32 β-strands across 4 chains. 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 | 54-70 | 17 | |
| 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 | 176-178 | 3 | |
| α-helix | 184-194 | 11 | |
| β-strand | 199-201 | 3 | 1 |
| α-helix | 202-210 | 9 | |
| 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 | 274-281 | 8 | |
| α-helix | 282-284 | 3 | |
| β-strand | 290-295 | 6 | 2 |
| β-strand | 300 | 1 | 3 |
| β-strand | 302 | 1 | 3 |
| β-strand | 303-308 | 6 | 2 |
| β-strand | 314-317 | 4 | 2 |
| α-helix | 324-333 | 10 | |
| β-strand | 339-340 | 2 | 2 |
| α-helix | 345-347 | 3 | |
| α-helix | 365-371 | 7 | |
| α-helix | 372-376 | 5 | |
| β-strand | 380 | 1 | 4 |
| β-strand | 388 | 1 | 4 |
| β-strand | 391-394 | 4 | 5 |
| β-strand | 399-400 | 2 | 5 |
| α-helix | 402-411 | 10 | |
| β-strand | 415 | 1 | 6 |
| β-strand | 422 | 1 | 6 |
| β-strand | 425-428 | 4 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7 | 1 | |
| β-strand | 8 | 1 | 2 |
| α-helix | 9-11 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 53-71 | 19 | |
| α-helix | 80 | 1 | |
| 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 | 7 |
| α-helix | 202-210 | 9 | |
| α-helix | 218-228 | 11 | |
| β-strand | 235-237 | 3 | 7 |
| α-helix | 238-247 | 10 | |
| α-helix | 251-253 | 3 | |
| α-helix | 254-258 | 5 | |
| α-helix | 259-263 | 5 | |
| β-strand | 268 | 1 | 8 |
| α-helix | 274-280 | 7 | |
| β-strand | 290-295 | 6 | 8 |
| β-strand | 303-308 | 6 | 8 |
| β-strand | 314-317 | 4 | 8 |
| α-helix | 324-333 | 10 | |
| β-strand | 339-340 | 2 | 8 |
| α-helix | 345-348 | 4 | |
| α-helix | 365-371 | 7 | |
| α-helix | 372-376 | 5 | |
| β-strand | 380 | 1 | 9 |
| β-strand | 388 | 1 | 9 |
| β-strand | 391-394 | 4 | 10 |
| β-strand | 399-400 | 2 | 10 |
| α-helix | 402-411 | 10 | |
| β-strand | 415 | 1 | 11 |
| β-strand | 422 | 1 | 11 |
| β-strand | 425-428 | 4 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| E3 ubiquitin-protein ligase | A, C | protein | 389 | HOMO SAPIENS | P22681 (AlphaFold model) |
| Tyrosine-protein kinase zap-70 zap-70,70 kda zeta-associated protein, syk-related tyrosine kinase | B, D | protein | 12 | HOMO SAPIENS | P43403 (AlphaFold model) |
>2Y1N_1 E3 UBIQUITIN-PROTEIN LIGASE (chains A, C) PPGTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRTILSRYEGKM ETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQPRRNLTKLSLIFSHMLAELK GIFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVPWKSFRQALHEVHPISSGLEAMALKS TIDLTCNDYISVFEFDIFTRLFQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIH KPGSYIFRLSCTRLGQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQN PDLTGLCEPTPQDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLT SWQESEGQGCPFCRCEIKGTEPIVVDPFD
>2Y1N_2 TYROSINE-PROTEIN KINASE ZAP-70 ZAP-70,70 KDA ZETA-ASSOCIATED PROTEIN, SYK-RELATED TYROSINE KINASE (chains B, D) TLNSDGYTPEPA
Structural Basis for Autoinhibition and Phosphorylation-Dependent Activation of C-Cbl. Dou, H., Buetow, L., Hock, A. et al. Nat Struct Mol Biol (2012) 19:184. DOI 10.1038/NSMB.2231 · PubMed
Other PDB entries of the same protein (UniProt P22681 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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