Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex. Determined by X-ray diffraction at 2.0 Å resolution. Released 27 Jan 2009.
Explore 3BVG in 3D Show helices and sheets RCSB PDB PDBe
3BVG contains 8 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 | 48-51 | 4 | 3 |
| β-strand | 63-67 | 5 | 3 |
| α-helix | 71-78 | 8 | |
| 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 |
| 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) |
>3BVG_1 Enterotoxin type C-3 (chains A) ESQPDPMPDDLHKSSEFTGTMGNMKYLYDDHYVSATKVKSVDKFLAHDLIYNISDKKLKN YDKVKTELLNEDLAKKYKDEVVDVYGSNYYVNCYFSSKDASTWHGKTCMYGGITKHEGNH FDNGNLQNVLVRVYENKRNTISFEVQTDKKSVTAQELDIKARNFLINKKNLYEFNSSPYE TGYIKFIENNGNTFWYDMMPAPGDKFDQSKYLMMYNDNKTVDSKSVKIEVHLTTKNG
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 1 |
Assessing energetic contributions to binding from a disordered region in a protein-protein interaction. Cho, S., Swaminathan, C.P., Bonsor, D.A. et al. Biochemistry (2010) 49:9256-9268. DOI 10.1021/bi1008968 · PubMed
Other PDB entries of the same protein (UniProt P0A0L5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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