Crystal structure of RaTG13 receptor-binding domain complexed with squirrel ACE2. Determined by X-ray diffraction at 2.76 Å resolution. Released 6 Aug 2025.
Explore 9JR4 in 3D Show helices and sheets RCSB PDB PDBe
9JR4 contains 48 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 | 25-52 | 28 | |
| α-helix | 56-81 | 26 | |
| α-helix | 85-87 | 3 | |
| α-helix | 91-102 | 12 | |
| α-helix | 110-113 | 4 | |
| α-helix | 115-128 | 14 | |
| β-strand | 131-134 | 4 | 1 |
| β-strand | 137-143 | 7 | 1 |
| α-helix | 144-148 | 5 | |
| α-helix | 149-154 | 6 | |
| α-helix | 158-193 | 36 | |
| α-helix | 199-204 | 6 | |
| α-helix | 205-207 | 3 | |
| 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 | 276-278 | 3 | |
| α-helix | 279-282 | 4 | |
| α-helix | 289-290 | 2 | |
| α-helix | 294-300 | 7 | |
| α-helix | 304-318 | 15 | |
| α-helix | 325-330 | 6 | |
| β-strand | 332 | 1 | 4 |
| α-helix | 335-336 | 2 | |
| β-strand | 347-350 | 4 | 4 |
| β-strand | 356-359 | 4 | 4 |
| α-helix | 366-384 | 19 | |
| α-helix | 390-392 | 3 | |
| α-helix | 398-412 | 15 | |
| α-helix | 415-420 | 6 | |
| α-helix | 432-465 | 34 | |
| 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 | 514-535 | 19 | |
| α-helix | 542-544 | 3 | |
| α-helix | 551-563 | 13 | |
| α-helix | 564-566 | 3 | |
| α-helix | 569-577 | 9 | |
| α-helix | 585-590 | 6 | |
| α-helix | 592-601 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 335 | 1 | 5 |
| α-helix | 336 | 1 | |
| α-helix | 338-342 | 5 | |
| β-strand | 348 | 1 | 6 |
| β-strand | 354-358 | 5 | 6 |
| β-strand | 361-363 | 3 | 5 |
| α-helix | 366-369 | 4 | |
| β-strand | 376-380 | 5 | 6 |
| α-helix | 384-386 | 3 | |
| β-strand | 391-392 | 2 | 5 |
| β-strand | 394-403 | 10 | 6 |
| α-helix | 404-408 | 5 | |
| α-helix | 417-421 | 5 | |
| β-strand | 431-437 | 7 | 6 |
| α-helix | 439-442 | 4 | |
| β-strand | 448 | 1 | 7 |
| β-strand | 452-454 | 3 | 8 |
| α-helix | 460-462 | 3 | |
| α-helix | 471-472 | 2 | |
| β-strand | 473-474 | 2 | 9 |
| β-strand | 485 | 1 | 9 |
| β-strand | 488-489 | 2 | 9 |
| β-strand | 492-494 | 3 | 8 |
| β-strand | 497 | 1 | 7 |
| α-helix | 503-505 | 3 | |
| β-strand | 507-516 | 10 | 6 |
| β-strand | 524-526 | 3 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Angiotensin-converting enzyme | B | protein | 597 | Petaurus norfolcensis | A0A8D2KIZ1 (AlphaFold model) |
| Spike glycoprotein | E | protein | 198 | Bat coronavirus RaTG13 | A0ABF7PLN6 |
>9JR4_1 Angiotensin-converting enzyme (chains B) STIEELAKTFLDKFNQEAEDLDHQRSLAAWNYNTNITKENTEKMNEAEAKWSAFYEEQSK LAKDYPLQEIQNFTLKRQLQALQQSGSSALSANKREQLNTILNTMSTIYSTGKVCNPKKP QECLLLEPGLDEIMANSTDYSERLWVWEGWRSEVGKQLRPLYEEYVVLKNEMARANNYED YGDYWRGDYEAEGADGYGYNRNQLIEDVERTFAEIKPLYEHLHAYVRAKLMNTYPSYISP TGCLPAHLLGDMWGRFWTNLYSLTVPFPEKPNIDVTDAMINQNWNAVRIFKEAEKFFVSV GLPNMTQGFWENSMLTEPTDGRKVVCHPTAWDLQKGDFRIKMCTKVTMDNFLTAHHEMGH IQYDMAYAMQPYLLRNGANEGFHEAVGEIMSLSASTPKHLKSIGLLPSDFREDNETEINF LLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVMEPVPHDETYC DPAALYHVSNDFSFIRYYTRTIYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLLNML RLGKSKPWTLALENVVGARNMDVRPLLNYFEPLFGWLKDQNRNSFVGWNTDWSPYTD
>9JR4_2 Spike glycoprotein (chains E) PTNLCPFGEVFNATTFASVYAWNRKRISNCVADYSVLYNSTSFSTFKCYGVSPTKLNDLC FTNVYADSFVITGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNSKHIDAKEGGNFNY LYRLFRKANLKPFERDISTEIYQAGSKPCNGQTGLNCYYPLYRYGFYPTDGVGHQPYRVV VLSFELLNAPATVCGHHH
Water and common crystallization additives (CL) are not listed.
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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