Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex. Determined by X-ray diffraction at 2.3 Å resolution. Released 12 May 2009.
Explore 3BVZ in 3D Show helices and sheets RCSB PDB PDBe
3BVZ contains 9 α-helices and 19 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 |
|---|---|---|---|
| α-helix | 2-7 | 6 | |
| α-helix | 8-10 | 3 | |
| α-helix | 14-16 | 3 | |
| β-strand | 17 | 1 | 1 |
| α-helix | 22-28 | 7 | |
| β-strand | 33-38 | 6 | 2 |
| β-strand | 42 | 1 | 3 |
| β-strand | 48-52 | 5 | 3 |
| β-strand | 63-67 | 5 | 3 |
| α-helix | 71-77 | 7 | |
| β-strand | 82-86 | 5 | 2 |
| β-strand | 89 | 1 | 3 |
| β-strand | 108-112 | 5 | 3 |
| β-strand | 115-117 | 3 | 2 |
| β-strand | 122 | 1 | 4 |
| β-strand | 129-137 | 9 | 5 |
| β-strand | 140-149 | 10 | 5 |
| β-strand | 151 | 1 | 4 |
| β-strand | 153-155 | 3 | 6 |
| α-helix | 156-171 | 16 | |
| β-strand | 181-189 | 9 | 5 |
| β-strand | 195-199 | 5 | 5 |
| α-helix | 202-203 | 2 | |
| β-strand | 205 | 1 | 1 |
| α-helix | 210-214 | 5 | |
| α-helix | 215-219 | 5 | |
| β-strand | 222-224 | 3 | 6 |
| β-strand | 229-236 | 8 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Enterotoxin type C-3 | A | protein | 237 | Staphylococcus aureus | P0A0L5 (AlphaFold model) |
>3BVZ_1 Enterotoxin type C-3 (chains A) ESQPDPMPDDLHKSSEFTGTMGNMKYLYDDHYVSATKVKSVDKFLAHDLIYNISDKKLKN YDKVKTELLNEDLAKKYKDEVVDVYGSNYYVNCYFSSKDNKWWHGKTCMYGGITKHEGNH FDNGNLQNVLVRVYENKRNTISFEVQTDKKSVTAQELDIKARNFLINKKNLYEFNSSPYE TGYIKFIENNGNTFWYDMMPAPGDKFDQSKYLMMYNDNKTVDSKSVKIEVHLTTKNG
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 1 |
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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