Engineering a misfolded form of rat CD2. Determined by X-ray diffraction at 2.0 Å resolution. Released 27 May 1998.
Explore 1A64 in 3D Show helices and sheets RCSB PDB PDBe
1A64 contains 6 α-helices and 18 β-strands across 2 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 |
|---|---|---|---|
| β-strand | 5-9 | 5 | 1 |
| β-strand | 14-16 | 3 | 2 |
| β-strand | 27-34 | 8 | 1 |
| β-strand | 37-43 | 7 | 1 |
| α-helix | 48 | 1 | |
| β-strand | 49-50 | 2 | 3 |
| β-strand | 55-57 | 3 | 4 |
| α-helix | 62 | 1 | |
| β-strand | 63-65 | 3 | 4 |
| α-helix | 70-72 | 3 | |
| β-strand | 74-82 | 9 | 3 |
| β-strand | 87-98 | 12 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CD2 | A, B | protein | 97 | Rattus norvegicus | P08921 (AlphaFold model) |
>1A64_1 CD2 (chains A, B) RDSGTVWGALGHGINLNIPNFQMTDDIDEVRWERGSTLVAEFKRKPFLKSGAFEILANGD LKIKNLTRDDSGTYNVTVYSTNGTRILDKALDLRILE
Engineering an intertwined form of CD2 for stability and assembly. Murray, A.J., Head, J.G., Barker, J.J. et al. Nat Struct Biol (1998) 5:778-782. DOI 10.1038/1816 · PubMed
Other PDB entries of the same protein (UniProt P08921 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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