BtHKU5-CoV-2-441 Spike RBD domain binding to hACE2. Determined by electron microscopy at 2.94 Å resolution. Released 12 Mar 2025.
Explore 9JJ6 in 3D Show helices and sheets RCSB PDB PDBe
9JJ6 contains 44 α-helices and 20 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 | 56-80 | 25 | |
| α-helix | 91-100 | 10 | |
| α-helix | 104-107 | 4 | |
| α-helix | 110-128 | 19 | |
| β-strand | 131-132 | 2 | 4 |
| β-strand | 142-143 | 2 | 4 |
| α-helix | 144-148 | 5 | |
| α-helix | 149-154 | 6 | |
| α-helix | 158-171 | 14 | |
| α-helix | 173-175 | 3 | |
| α-helix | 177-192 | 16 | |
| α-helix | 199-204 | 6 | |
| α-helix | 205-207 | 3 | |
| β-strand | 209 | 1 | 5 |
| β-strand | 217 | 1 | 5 |
| α-helix | 221-249 | 29 | |
| β-strand | 262-263 | 2 | 6 |
| α-helix | 264-266 | 3 | |
| α-helix | 276-278 | 3 | |
| α-helix | 279-282 | 4 | |
| α-helix | 289-291 | 3 | |
| α-helix | 294-299 | 6 | |
| α-helix | 304-318 | 15 | |
| α-helix | 320-324 | 5 | |
| α-helix | 325-330 | 6 | |
| β-strand | 347-352 | 6 | 7 |
| β-strand | 355-359 | 5 | 7 |
| α-helix | 366-385 | 20 | |
| α-helix | 390-392 | 3 | |
| α-helix | 400-412 | 13 | |
| α-helix | 415-420 | 6 | |
| α-helix | 432-445 | 14 | |
| α-helix | 449-464 | 16 | |
| α-helix | 470-472 | 3 | |
| α-helix | 473-480 | 8 | |
| α-helix | 481-485 | 5 | |
| β-strand | 487-488 | 2 | 6 |
| α-helix | 500-502 | 3 | |
| α-helix | 504-507 | 4 | |
| α-helix | 514-532 | 19 | |
| α-helix | 548-558 | 11 | |
| α-helix | 566-574 | 9 | |
| α-helix | 582-587 | 6 | |
| α-helix | 589-598 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 379-382 | 4 | |
| α-helix | 385-387 | 3 | |
| β-strand | 388 | 1 | 1 |
| α-helix | 389-391 | 3 | |
| α-helix | 392 | 1 | |
| β-strand | 393-397 | 5 | 1 |
| α-helix | 404-409 | 6 | |
| β-strand | 411 | 1 | 2 |
| β-strand | 415-419 | 5 | 1 |
| β-strand | 433-440 | 8 | 1 |
| α-helix | 443-449 | 7 | |
| β-strand | 470-475 | 6 | 1 |
| β-strand | 477 | 1 | 2 |
| β-strand | 489-499 | 11 | 3 |
| β-strand | 502-505 | 4 | 3 |
| α-helix | 507-509 | 3 | |
| β-strand | 523-526 | 4 | 3 |
| β-strand | 533-541 | 9 | 3 |
| β-strand | 549-556 | 8 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| BtHKU5-CoV-2-441 Spike RBD domain | B | protein | 239 | Pipistrellus bat coronavirus HKU5 | A3EXD0 (AlphaFold model) |
| Processed angiotensin-converting enzyme 2 | A | protein | 608 | Homo sapiens | Q9BYF1 (AlphaFold model) |
>9JJ6_1 BtHKU5-CoV-2-441 Spike RBD domain (chains B) MDAMKRGLCCVLLLCGAVFVSAAKSRGKFIEQPKVQECDFSPLLTGTPPQVYNFNRLSFT NCNYNLTKLLSLFEVSEFSCNAISPSALASTCYSSLTVDYFAFPLSMASYLRPGSTGPTA EFNYRQDFSNPTCRVLATPSSNITITKPSNYNWIRLCRTTGAFGNRDQKVQPGHYSRCRY IAPTGSIYLGGNEGYLVSDGQSASMTERVQMTFVISVTFGTESNSVCPAAAHHHHHHHH
>9JJ6_2 Processed angiotensin-converting enzyme 2 (chains A) STIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGDKWSAFLKEQST LAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNP QECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLYEEYVVLKNEMARANHYED YGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYISP IGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFKEAEKFFVSV GLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMGH IQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKSIGLLSPDFQEDNETEINF LLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETYC DPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLFNML RLGKSEPWTLALENVVGAKNMNVRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPYADAAA HHHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 6 |
Bat-infecting merbecovirus HKU5-CoV lineage 2 can use human ACE2 as a cell entry receptor. Chen, J., Zhang, W., Li, Y. et al. Cell (2025) 188:1729-1742.e16. DOI 10.1016/j.cell.2025.01.042 · PubMed
Other PDB entries of the same protein (UniProt A3EXD0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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