Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex. Determined by X-ray diffraction at 2.2 Å resolution. Released 12 May 2009.
Explore 3BYY in 3D Show helices and sheets RCSB PDB PDBe
3BYY contains 10 α-helices and 32 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 | 4-7 | 4 | 1 |
| β-strand | 10-13 | 4 | 2 |
| β-strand | 19-21 | 3 | 3 |
| β-strand | 22-25 | 4 | 1 |
| β-strand | 31-37 | 7 | 2 |
| β-strand | 43-51 | 9 | 2 |
| β-strand | 54-57 | 4 | 2 |
| β-strand | 66-68 | 3 | 3 |
| β-strand | 74 | 1 | 1 |
| β-strand | 76-79 | 4 | 3 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-95 | 8 | 2 |
| β-strand | 100-108 | 3 | 2 |
| β-strand | 112-116 | 5 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-7 | 5 | |
| α-helix | 8-10 | 3 | |
| α-helix | 14-16 | 3 | |
| β-strand | 17 | 1 | 4 |
| α-helix | 22-25 | 4 | |
| β-strand | 33-38 | 6 | 5 |
| β-strand | 42 | 1 | 6 |
| β-strand | 48-52 | 5 | 6 |
| β-strand | 63-67 | 5 | 6 |
| α-helix | 71-77 | 7 | |
| β-strand | 82-86 | 5 | 5 |
| β-strand | 89 | 1 | 6 |
| β-strand | 106-110 | 5 | 6 |
| β-strand | 113-115 | 3 | 5 |
| β-strand | 120 | 1 | 7 |
| β-strand | 127-135 | 9 | 8 |
| β-strand | 138-147 | 10 | 8 |
| β-strand | 149 | 1 | 7 |
| β-strand | 151-153 | 3 | 9 |
| α-helix | 154-169 | 16 | |
| β-strand | 179-187 | 9 | 8 |
| β-strand | 193-197 | 5 | 8 |
| α-helix | 200-201 | 2 | |
| β-strand | 203 | 1 | 4 |
| α-helix | 208-212 | 5 | |
| α-helix | 213-217 | 5 | |
| β-strand | 220-222 | 3 | 9 |
| β-strand | 227-234 | 8 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| T cell receptor beta chain 8.2 | A | protein | 109 | Mus musculus | |
| Enterotoxin type C-3 | B | protein | 237 | Staphylococcus aureus | P0A0L5 (AlphaFold model) |
>3BYY_1 T cell receptor beta chain 8.2 (chains A) AAVTQSPRNKVAVTGEKVTLSCQQTNNHNNMYWYRQDTGHGLRLIHYSYGAGSTEKGDIP DGYKASRPSQEQFSLILESATPSQTSVYFCASGGGGTLYFGAGTRLSVL
>3BYY_2 Enterotoxin type C-3 (chains B) ESQPDPMPDDLHKSSEFTGTMGNMKYLYDDHYVSATKVKSVDKFLAHDLIYNISDKKLKN YDKVKTELLNEDLAKKYKDEVVDVYGSNYYVNCYFSSKDNVWWPGKTCMYGGITKHEGNH FDNGNLQNVLVRVYENKRNTISFEVQTDKKSVTAQELDIKARNFLINKKNLYEFNSSPYE TGYIKFIENNGNTFWYDMMPAPGDKFDQSKYLMMYNDNKTVDSKSVKIEVHLTTKNG
Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex. Cho, S., Swaminathan, C.P., Kerzic, M.C. et al. To be published.
Other PDB entries of the same protein (UniProt P0A0L5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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