Crystal structure of SARS-CoV-2 receptor-binding domain complexed with squirrel ACE2. Determined by X-ray diffraction at 3.16 Å resolution. Released 6 Aug 2025.
Explore 9JRC in 3D Show helices and sheets RCSB PDB PDBe
9JRC contains 48 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 | 91-101 | 11 | |
| α-helix | 110-115 | 6 | |
| α-helix | 118-129 | 12 | |
| β-strand | 131-134 | 4 | 1 |
| β-strand | 137-143 | 7 | 1 |
| α-helix | 144-148 | 5 | |
| α-helix | 149-154 | 6 | |
| α-helix | 158-171 | 14 | |
| α-helix | 173-193 | 21 | |
| α-helix | 199-203 | 5 | |
| α-helix | 204-207 | 4 | |
| β-strand | 209 | 1 | 2 |
| β-strand | 217 | 1 | 2 |
| α-helix | 219-251 | 33 | |
| α-helix | 261 | 1 | |
| β-strand | 262-263 | 2 | 3 |
| α-helix | 264-266 | 3 | |
| α-helix | 275-278 | 4 | |
| α-helix | 279-282 | 4 | |
| α-helix | 294-299 | 6 | |
| α-helix | 304-318 | 15 | |
| α-helix | 320-324 | 5 | |
| α-helix | 325-330 | 6 | |
| β-strand | 332 | 1 | 4 |
| β-strand | 347-350 | 4 | 4 |
| β-strand | 356-359 | 4 | 4 |
| α-helix | 366-384 | 19 | |
| α-helix | 385-387 | 3 | |
| α-helix | 390-392 | 3 | |
| α-helix | 400-413 | 14 | |
| α-helix | 415-421 | 7 | |
| α-helix | 432-464 | 33 | |
| α-helix | 470-472 | 3 | |
| α-helix | 473-480 | 8 | |
| α-helix | 481-485 | 5 | |
| β-strand | 487-488 | 2 | 3 |
| α-helix | 499-502 | 4 | |
| α-helix | 504-507 | 4 | |
| α-helix | 513-535 | 20 | |
| α-helix | 542-544 | 3 | |
| α-helix | 551-561 | 11 | |
| α-helix | 564-566 | 3 | |
| α-helix | 569-577 | 9 | |
| α-helix | 585-601 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 335 | 1 | 5 |
| α-helix | 338-342 | 5 | |
| β-strand | 349 | 1 | 6 |
| α-helix | 350-352 | 3 | |
| β-strand | 354-358 | 5 | 6 |
| β-strand | 361-362 | 2 | 5 |
| α-helix | 366-369 | 4 | |
| β-strand | 376-380 | 5 | 6 |
| α-helix | 385-389 | 5 | |
| β-strand | 391-392 | 2 | 5 |
| β-strand | 394-403 | 10 | 6 |
| α-helix | 404-409 | 6 | |
| α-helix | 417-421 | 5 | |
| β-strand | 431-437 | 7 | 6 |
| α-helix | 439-442 | 4 | |
| β-strand | 452-454 | 3 | 7 |
| α-helix | 460-462 | 3 | |
| α-helix | 471-472 | 2 | |
| β-strand | 473-474 | 2 | 8 |
| β-strand | 485 | 1 | 8 |
| β-strand | 488-489 | 2 | 8 |
| β-strand | 492-494 | 3 | 7 |
| α-helix | 503-505 | 3 | |
| β-strand | 507-516 | 10 | 6 |
| β-strand | 524-525 | 2 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Angiotensin-converting enzyme | B | protein | 593 | Petaurus norfolcensis | A0A8D2KIZ1 (AlphaFold model) |
| Spike protein S1 | E | protein | 196 | Severe acute respiratory syndrome coronavirus 2 | P0DTC2 (AlphaFold model) |
>9JRC_1 Angiotensin-converting enzyme (chains B) PSTIEELAKTFLDKFNQEAEDLDHQRSLAAWNYNTNITKENTEKMNEAEAKWSAFYEEQS KLAKDYPLQEIQNFTLKRQLQALQQSGSSALSANKREQLNTILNTMSTIYSTGKVCNPKK PQECLLLEPGLDEIMANSTDYSERLWVWEGWRSEVGKQLRPLYEEYVVLKNEMARANNYE DYGDYWRGDYEAEGADGYGYNRNQLIEDVERTFAEIKPLYEHLHAYVRAKLMNTYPSYIS PTGCLPAHLLGDMWGRFWTNLYSLTVPFPEKPNIDVTDAMINQNWNAVRIFKEAEKFFVS VGLPNMTQGFWENSMLTEPTDGRKVVCHPTAWDLQKGDFRIKMCTKVTMDNFLTAHHEMG HIQYDMAYAMQPYLLRNGANEGFHEAVGEIMSLSASTPKHLKSIGLLPSDFREDNETEIN FLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVMEPVPHDETY CDPAALYHVSNDFSFIRYYTRTIYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLLNM LRLGKSKPWTLALENVVGARNMDVRPLLNYFEPLFGWLKDQNRNSFVGWNTDW
>9JRC_2 Spike protein S1 (chains E) TNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSTSFSTFKCYGVSPTKLNDLCF TNVYADSFVIRGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYL YRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFPLQSYGFQPTNGVGYQPYRVVV LSFELLHAPATVCGPH
Cross-species recognition of squirrel ACE2 by the receptor binding domains of SARS-CoV-2, RaTG13, PCoV-GD and PCoV-GX. Wang, C., Nan, X., Deng, Y. et al. Structure (2025) 33:1750-1759.e2. DOI 10.1016/j.str.2025.07.003 · PubMed
Other PDB entries of the same protein (UniProt A0A8D2KIZ1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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