Solution structure of the second SH3 domain of Human CMS protein. Determined by solution NMR. Released 5 Dec 2006.
Explore 2FEI in 3D Show helices and sheets RCSB PDB PDBe
2FEI 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 | 3-5 | 3 | 1 |
| β-strand | 17 | 1 | 1 |
| β-strand | 25-27 | 3 | 1 |
| β-strand | 36-40 | 5 | 1 |
| β-strand | 45-49 | 5 | 1 |
| β-strand | 55 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CD2-associated protein | A | protein | 65 | Homo sapiens | Q9Y5K6 (AlphaFold model) |
>2FEI_1 CD2-associated protein (chains A) MRQCKVLFEYIPQNEDELELKVGDIIDINEEVEEGWWSGTLNNKLGLFPSNFVKELELEH HHHHH
Solution structure of the second SH3 domain of human CMS and a newly identified binding site at the C-terminus of c-Cbl. Yao, B., Zhang, J., Dai, H. et al. Biochim Biophys Acta (2007) 1774:35-43. DOI 10.1016/j.bbapap.2006.09.018 · PubMed
Other PDB entries of the same protein (UniProt Q9Y5K6 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2FEI directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.