Solution structure of a circular form of the N-terminal SH3 domain (E132C, E133G, R191G mutant) from oncogene protein c-Crk. Determined by solution NMR. Released 5 Aug 2003.
Explore 1M3C in 3D Show helices and sheets RCSB PDB PDBe
1M3C contains 0 α-helices and 6 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 |
|---|---|---|---|
| β-strand | 136-139 | 4 | 1 |
| β-strand | 150 | 1 | 1 |
| β-strand | 157-163 | 7 | 1 |
| β-strand | 169-173 | 5 | 1 |
| β-strand | 179-183 | 5 | 1 |
| β-strand | 187-189 | 3 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Proto-oncogene C-crk | A | protein | 60 | Mus musculus | Q64010 (AlphaFold model) |
>1M3C_1 Proto-oncogene C-crk (chains A) CGAEYVRALFDFNGNDEEDLPFKKGDILRIRDKPEEQWWNAEDSEGKRGMIPVPYVEKYG
Changing protein backbone topology: Structural and dynamic consequences of the backbone cyclization in SH3 domain. Schumann, F.H., Varadan, R., Tayakuniyil, P.P. et al. To be published.
Other PDB entries of the same protein (UniProt Q64010 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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