SARS-CoV-2 Omicron BF.7 RBD complexed with human ACE2. Determined by electron microscopy at 2.47 Å resolution. Released 24 Jul 2024.
Explore 8WE1 in 3D Show helices and sheets RCSB PDB PDBe
8WE1 contains 45 α-helices and 26 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 | 21-52 | 32 | |
| α-helix | 56-79 | 24 | |
| α-helix | 80-82 | 3 | |
| α-helix | 85-87 | 3 | |
| α-helix | 93-100 | 8 | |
| α-helix | 104-106 | 3 | |
| α-helix | 110-128 | 19 | |
| β-strand | 132 | 1 | 1 |
| β-strand | 142 | 1 | 1 |
| α-helix | 144-148 | 5 | |
| α-helix | 149-153 | 5 | |
| α-helix | 158-171 | 14 | |
| α-helix | 173-175 | 3 | |
| α-helix | 177-193 | 17 | |
| α-helix | 199-204 | 6 | |
| α-helix | 205-207 | 3 | |
| β-strand | 209 | 1 | 2 |
| β-strand | 217 | 1 | 2 |
| α-helix | 221-248 | 28 | |
| α-helix | 261 | 1 | |
| β-strand | 262-263 | 2 | 3 |
| α-helix | 276-278 | 3 | |
| α-helix | 289-291 | 3 | |
| α-helix | 294-298 | 5 | |
| α-helix | 304-316 | 13 | |
| α-helix | 320-324 | 5 | |
| α-helix | 325-330 | 6 | |
| β-strand | 347-352 | 6 | 4 |
| β-strand | 355-359 | 5 | 4 |
| α-helix | 366-384 | 19 | |
| α-helix | 390-392 | 3 | |
| α-helix | 401-410 | 10 | |
| α-helix | 411-413 | 3 | |
| α-helix | 415-420 | 6 | |
| α-helix | 429-431 | 3 | |
| α-helix | 432-446 | 15 | |
| α-helix | 450-465 | 16 | |
| α-helix | 473-480 | 8 | |
| α-helix | 481-485 | 5 | |
| β-strand | 487-488 | 2 | 3 |
| α-helix | 500-502 | 3 | |
| α-helix | 504-507 | 4 | |
| α-helix | 513-532 | 20 | |
| α-helix | 539-541 | 3 | |
| α-helix | 548-558 | 11 | |
| α-helix | 566-574 | 9 | |
| α-helix | 582-587 | 6 | |
| α-helix | 589-598 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 335 | 1 | 5 |
| β-strand | 354-358 | 5 | 6 |
| β-strand | 362 | 1 | 5 |
| β-strand | 376 | 1 | 6 |
| β-strand | 379-380 | 2 | 7 |
| α-helix | 386-388 | 3 | |
| β-strand | 392 | 1 | 8 |
| β-strand | 394-402 | 9 | 6 |
| α-helix | 404-409 | 6 | |
| α-helix | 417-420 | 4 | |
| β-strand | 431-432 | 2 | 7 |
| β-strand | 433-437 | 5 | 6 |
| β-strand | 448 | 1 | 9 |
| β-strand | 452-454 | 3 | 10 |
| α-helix | 471-472 | 2 | |
| β-strand | 473-474 | 2 | 11 |
| β-strand | 485 | 1 | 11 |
| β-strand | 488-489 | 2 | 11 |
| β-strand | 492-494 | 3 | 10 |
| β-strand | 497 | 1 | 9 |
| β-strand | 508-516 | 9 | 6 |
| α-helix | 521-522 | 2 | |
| β-strand | 524 | 1 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Angiotensin-converting enzyme 2 | A | protein | 805 | Homo sapiens | Q9BYF1 (AlphaFold model) |
| Spike protein S2' | B | protein | 223 | Severe acute respiratory syndrome coronavirus 2 | P0DTC2 (AlphaFold model) |
>8WE1_1 Angiotensin-converting enzyme 2 (chains A) MSSSSWLLLSLVAVTAAQSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQ NMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTIL NTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLY EEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHL HAYVRAKLMNAYPSYISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQ AWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDFRILM CTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKS IGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEM KREIVGVVEPVPHDETYCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLH KCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGAKNMNVRPLLNYFEPLFTWLKDQNK NSFVGWSTDWSPYADQSIKVRISLKSALGDKAYEWNDNEMYLFRSSVAYAMRQYFLKVKN QMILFGEEDVRVANLKPRISFNFFVTAPKNVSDIIPRTEVEKAIRMSRSRINDAFRLNDN SLEFLGIQPTLGPPNQPPVSIWLIVFGVVMGVIVVGIVILIFTGIRDRKKKNKARSGENP YASIDISKGENNPGFQNTDDVQTSF
>8WE1_2 Spike protein S2' (chains B) RVQPTESIVRFPNITNLCPFDEVFNATTFASVYAWNRKRISNCVADYSVLYNFAPFFAFK CYGVSPTKLNDLCFTNVYADSFVIRGNEVSQIAPGQTGNIADYNYKLPDDFTGCVIAWNS NKLDSKVGGNYNYRYRLFRKSNLKPFERDISTEIYQAGNKPCNGVAGVNCYFPLQSYGFR PTYGVGHQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNF
Key mechanistic features of the trade-off between antibody escape and host cell binding in the SARS-CoV-2 Omicron variant spike proteins. Li, W., Xu, Z., Niu, T. et al. EMBO J (2024) 43:1484-1498. DOI 10.1038/s44318-024-00062-z · PubMed
Other PDB entries of the same protein (UniProt Q9BYF1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 8WE1 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.