Crystal structure of the scFv antibody 4B08 with epitope peptide (mutation N3A). Determined by X-ray diffraction at 1.96 Å resolution. Released 6 Jun 2018.
Explore 5YD5 in 3D Show helices and sheets RCSB PDB PDBe
5YD5 contains 15 α-helices and 50 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 | 5-8 | 4 | 1 |
| α-helix | 9-11 | 3 | |
| β-strand | 12-14 | 3 | 2 |
| β-strand | 20-27 | 8 | 1 |
| β-strand | 36-41 | 6 | 2 |
| β-strand | 47-53 | 7 | 2 |
| β-strand | 60-62 | 3 | 2 |
| α-helix | 64-66 | 3 | |
| β-strand | 70-75 | 6 | 1 |
| β-strand | 80-85 | 6 | 1 |
| α-helix | 90-92 | 3 | |
| β-strand | 94-102 | 9 | 2 |
| β-strand | 105-109 | 5 | 2 |
| β-strand | 113-117 | 5 | 2 |
| β-strand | 122 | 1 | 2 |
| α-helix | 140-143 | 4 | |
| β-strand | 144-145 | 2 | 3 |
| β-strand | 150-153 | 4 | 4 |
| β-strand | 159-165 | 7 | 3 |
| β-strand | 170 | 1 | 5 |
| β-strand | 176 | 1 | 5 |
| β-strand | 178-183 | 6 | 4 |
| β-strand | 190-194 | 5 | 4 |
| β-strand | 198-199 | 2 | 4 |
| α-helix | 200 | 1 | |
| β-strand | 207-211 | 5 | 3 |
| β-strand | 215-220 | 6 | 3 |
| α-helix | 225-227 | 3 | |
| β-strand | 229-235 | 7 | 4 |
| α-helix | 241 | 1 | |
| β-strand | 242-243 | 2 | 4 |
| β-strand | 247-251 | 5 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-8 | 4 | 6 |
| α-helix | 9-11 | 3 | |
| β-strand | 12-14 | 3 | 7 |
| β-strand | 20-27 | 8 | 6 |
| α-helix | 31-33 | 3 | |
| β-strand | 36-41 | 6 | 7 |
| β-strand | 47-53 | 7 | 7 |
| β-strand | 60-62 | 3 | 7 |
| α-helix | 64-66 | 3 | |
| β-strand | 70-75 | 6 | 6 |
| β-strand | 80-85 | 6 | 6 |
| α-helix | 90-92 | 3 | |
| β-strand | 94-102 | 9 | 7 |
| β-strand | 105-109 | 5 | 7 |
| β-strand | 113-117 | 5 | 7 |
| β-strand | 122 | 1 | 7 |
| α-helix | 140-143 | 4 | |
| β-strand | 144-145 | 2 | 8 |
| β-strand | 150-153 | 4 | 9 |
| β-strand | 159-165 | 7 | 8 |
| β-strand | 170 | 1 | 10 |
| β-strand | 176 | 1 | 10 |
| β-strand | 178-183 | 6 | 9 |
| β-strand | 190-194 | 5 | 9 |
| β-strand | 198-199 | 2 | 9 |
| α-helix | 200 | 1 | |
| β-strand | 207-211 | 5 | 8 |
| β-strand | 215-220 | 6 | 8 |
| α-helix | 225-227 | 3 | |
| β-strand | 229-235 | 7 | 9 |
| α-helix | 241 | 1 | |
| β-strand | 242-243 | 2 | 9 |
| β-strand | 247-251 | 5 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| scFv 4B08 | A, C | protein | 251 | Mus musculus | P01630 (AlphaFold model) |
| Peptide epitope (mutation N3A) | B, D | protein | 9 | Homo sapiens | P51681 (AlphaFold model) |
>5YD5_1 scFv 4B08 (chains A, C) EVQLQQSGAELVRPGTSVKMSCKAAGYTFTKYWIGWVKQRPGHGLEWIGDIHPGSFYSNY NEKFKGKATLTADTSSSTAYMQLSSLTSEDSAIYYCARDYYTNYGDWGQGTSVTVSSAGG GGSGGGGSGGGGSGGGGSDIVMTQAAPSVSVTPGESVSISCRSSKSLLHRNGNTYLFWFL QRPGQSPQLLIYRMSNLASGVPDRFSGSGSGTAFTLRISRVEAEDVGVYYCMQHLEYPYT FGSGTKLELKV
>5YD5_2 Peptide epitope (mutation N3A) (chains B, D) DIAYYTSEP
Intramolecular H-bonds govern the recognition of a flexible peptide by an antibody. Miyanabe, K., Akiba, H., Kuroda, D. et al. J Biochem (2018) 164:65-76. DOI 10.1093/jb/mvy032 · PubMed
Other PDB entries of the same protein (UniProt P01630 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 5YD5 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.