Structure of the HKU5 RBD bound to the P. abramus ACE2 receptor. Determined by electron microscopy at 3.1 Å resolution. Released 19 Feb 2025.
Explore 9D32 in 3D Show helices and sheets RCSB PDB PDBe
9D32 contains 49 α-helices and 24 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 | 21-51 | 31 | |
| α-helix | 56-80 | 25 | |
| α-helix | 85-87 | 3 | |
| α-helix | 93-100 | 8 | |
| α-helix | 104-107 | 4 | |
| α-helix | 111-128 | 18 | |
| β-strand | 131-133 | 3 | 1 |
| β-strand | 141-143 | 3 | 1 |
| α-helix | 144-151 | 8 | |
| α-helix | 157-170 | 14 | |
| α-helix | 176-192 | 17 | |
| α-helix | 198-203 | 6 | |
| α-helix | 204-206 | 3 | |
| β-strand | 208 | 1 | 2 |
| β-strand | 216 | 1 | 2 |
| α-helix | 221-250 | 30 | |
| α-helix | 260 | 1 | |
| β-strand | 261-262 | 2 | 3 |
| α-helix | 263-265 | 3 | |
| α-helix | 275-277 | 3 | |
| α-helix | 278-281 | 4 | |
| α-helix | 288-290 | 3 | |
| α-helix | 293-298 | 6 | |
| α-helix | 303-316 | 14 | |
| α-helix | 324-329 | 6 | |
| β-strand | 331 | 1 | 4 |
| β-strand | 346-349 | 4 | 4 |
| β-strand | 355-358 | 4 | 4 |
| α-helix | 365-383 | 19 | |
| α-helix | 389-391 | 3 | |
| α-helix | 399-411 | 13 | |
| α-helix | 414-420 | 7 | |
| α-helix | 431-445 | 15 | |
| α-helix | 446-448 | 3 | |
| α-helix | 449-464 | 16 | |
| α-helix | 469-471 | 3 | |
| α-helix | 472-479 | 8 | |
| α-helix | 480-484 | 5 | |
| β-strand | 486-487 | 2 | 3 |
| α-helix | 499-501 | 3 | |
| α-helix | 503-506 | 4 | |
| α-helix | 513-531 | 19 | |
| α-helix | 538-540 | 3 | |
| α-helix | 547-557 | 11 | |
| α-helix | 565-573 | 9 | |
| α-helix | 581-586 | 6 | |
| α-helix | 588-598 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 400 | 1 | 5 |
| α-helix | 401-404 | 4 | |
| α-helix | 405-407 | 3 | |
| β-strand | 409-413 | 5 | 6 |
| β-strand | 417 | 1 | 7 |
| α-helix | 424-426 | 3 | |
| β-strand | 428-435 | 8 | 6 |
| α-helix | 439-442 | 4 | |
| β-strand | 447 | 1 | 8 |
| β-strand | 449-456 | 8 | 6 |
| α-helix | 459-464 | 6 | |
| α-helix | 472 | 1 | |
| α-helix | 473-477 | 5 | |
| β-strand | 486-492 | 7 | 6 |
| α-helix | 493-494 | 2 | |
| β-strand | 500 | 1 | 5 |
| α-helix | 501-503 | 3 | |
| β-strand | 505-516 | 12 | 9 |
| β-strand | 519-522 | 4 | 9 |
| α-helix | 525-526 | 2 | |
| α-helix | 534-537 | 4 | |
| β-strand | 546-549 | 4 | 9 |
| β-strand | 553-561 | 9 | 9 |
| β-strand | 567-575 | 9 | 6 |
| β-strand | 583 | 1 | 8 |
| β-strand | 584 | 1 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Angiotensin-converting enzyme | A | protein | 768 | Pipistrellus abramus | C7ECT9 (AlphaFold model) |
| Spike glycoprotein | B | protein | 267 | Pipistrellus bat coronavirus HKU5 | A3EXD0 (AlphaFold model) |
>9D32_1 Angiotensin-converting enzyme (chains A) MPMGSLQPLATLYLLGMLVASVLAQYTTEEEARRFLVKFNHEAENLSHESALASWDYNTN ITDENAKKMNEADNKWSDFYKEQSKIAQGFPLQEIKDPIIKLQLQILQQNGSSVLTAEKR KRLSTILTTMSTIYSTGKVCNPNNPQQCFTLSGLEDIMEKSKDYHERLWVWEGWRSEVGK QLRPLYEEYVELKNEMARGNNYKDYGDYWRGDYETEGEKGYNYSRNYLMEDVDRIFLEIK PLYEQLHAYVRAKLMKAYPSHISPTGCLPAHLLGDMWGRFWTNLYNLTVPLEKEPNIDVT DTMKKQSWDAEKIFKEAEKFYSSVGLPNMTPGFWRDSMLTEPSDGRQVVCHPTAWDLGKN DFRIKMCTKVTMDDFLTAHHEMGHIQYDMAYANQSYLLRNGANEGFHEAVGEVMSLSVAT PKHLKGMGLLPSDFSENNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFEGKIPKEQWM EKWWEMKREIVGVVEPLPHDETYCDPASLFHVANDYSFIRYFTRTILEFQFQEALCRTAK HQGPLHKCDISNSTEAGKKLNDMLKLGKSTPWTYALEKIAETKEMDAKPLLNYFNPLFRW LKEQNGNSVGWSVDSSPYSNQSIKVRISLKSALGEKAYEWNENEMYLFQSSVAYAMRVYF LKAKNESIPFRAEDVRVSDEKKRVSFKFFVTSPTNMSDIIPRSEVEDAIRMSRSRINDAF RLDDNTLEFLGLVPRGSSSGGSGLNDIFEAQKIEWHEGGSHHHHHHHH
>9D32_2 Spike glycoprotein (chains B) MGILPSPGMPALLSLVSLLSVLLMGCVAETGTQECDFTPMLTGTPPPIYNFKRLVFTNCN YNLTKLLSLFQVSEFSCHQVSPSSLATGCYSSLTVDYFAYSTDMSSYLQPGSAGEIVQFN YKQDFSNPTCRVLATVPQNLTTITKPSNYAYLTECYKTSAYGKNYLYNAPGGYTPCLSLA SRGFSTKYQSHSDGELTTTGYIYPVTGNLQMAFIISVQYGTDTNSVCPMQLVPRGSSSGG SGLNDIFEAQKIEWHEGGSHHHHHHHH
Molecular basis of convergent evolution of ACE2 receptor utilization among HKU5 coronaviruses. Park, Y.J., Liu, C., Lee, J. et al. Cell (2025) 188:1711-1728.e21. DOI 10.1016/j.cell.2024.12.032 · PubMed
Other PDB entries of the same protein (UniProt C7ECT9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 9D32 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.