cryo-EM structure of omicron spike in complex with de novo designed binder, local. Determined by electron microscopy at 3.29 Å resolution. Released 1 Mar 2023.
Explore 7ZSD in 3D Show helices and sheets RCSB PDB PDBe
7ZSD contains 16 α-helices and 10 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 |
|---|---|---|---|
| α-helix | 334 | 1 | |
| β-strand | 335 | 1 | 1 |
| α-helix | 336 | 1 | |
| α-helix | 338-342 | 5 | |
| α-helix | 347-349 | 3 | |
| α-helix | 350-352 | 3 | |
| β-strand | 354-358 | 5 | 2 |
| β-strand | 362 | 1 | 1 |
| α-helix | 366-370 | 5 | |
| β-strand | 376 | 1 | 2 |
| β-strand | 379-380 | 2 | 2 |
| α-helix | 384-389 | 6 | |
| β-strand | 395-403 | 9 | 2 |
| α-helix | 404-409 | 6 | |
| α-helix | 417 | 1 | |
| α-helix | 418-422 | 5 | |
| β-strand | 431-437 | 7 | 2 |
| β-strand | 452-454 | 3 | 3 |
| α-helix | 460-462 | 3 | |
| α-helix | 471-473 | 3 | |
| β-strand | 492-494 | 3 | 3 |
| β-strand | 507-514 | 8 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-23 | 20 | |
| α-helix | 27-48 | 22 | |
| α-helix | 51-54 | 4 | |
| α-helix | 59-61 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Spike glycoprotein | M | protein | 196 | Severe acute respiratory syndrome coronavirus 2 | P0DTC2 (AlphaFold model) |
| de novo designed binder | P | protein | 79 | Drosophila melanogaster | Q9VKJ9 (AlphaFold model) |
>7ZSD_1 Spike glycoprotein (chains M) ITNLCPFDEVFNATRFASVYAWNRKRISNCVADYSVLYNLAPFFTFKCYGVSPTKLNDLC FTNVYADSFVIRGDEVRQIAPGQTGNIADYNYKLPDDFTGCVIAWNSNKLDSKVSGNYNY LYRLFRKSNLKPFERDISTEIYQAGNKPCNGVAGFNCYFPLRSYSFRPTYGVGHQPYRVV VLSFELLHAPATVCGP
>7ZSD_2 de novo designed binder (chains P) ETGASSTNMLEALQQRLQFYHGQVARAALENNSGKARRFGRIVKQYEDAIKLYKAGKPVP YDELPVPPGFGGSENLYFQ
De novo design of protein interactions with learned surface fingerprints. Gainza, P., Wehrle, S., Van Hall-Beauvais, A. et al. Nature (2023) 617:176-184. DOI 10.1038/s41586-023-05993-x · PubMed
Other PDB entries of the same protein (UniProt P0DTC2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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