Crystal structure of RaTG13 RBD complexed with sheep ACE2. Determined by X-ray diffraction at 3.74 Å resolution. Released 26 Nov 2025.
Explore 9KOS in 3D Show helices and sheets RCSB PDB PDBe
9KOS contains 52 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 | 21-53 | 33 | |
| α-helix | 56-80 | 25 | |
| α-helix | 85-87 | 3 | |
| α-helix | 91-100 | 10 | |
| α-helix | 104-107 | 4 | |
| α-helix | 110-129 | 20 | |
| β-strand | 131-133 | 3 | 1 |
| β-strand | 140-142 | 3 | 1 |
| α-helix | 149-153 | 5 | |
| α-helix | 157-170 | 14 | |
| α-helix | 172-192 | 21 | |
| α-helix | 198-203 | 6 | |
| β-strand | 208 | 1 | 2 |
| β-strand | 216 | 1 | 2 |
| α-helix | 220-250 | 31 | |
| α-helix | 252-254 | 3 | |
| 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 | 293-298 | 6 | |
| α-helix | 303-315 | 13 | |
| α-helix | 319-323 | 5 | |
| α-helix | 324-329 | 6 | |
| β-strand | 331 | 1 | 4 |
| β-strand | 346-351 | 6 | 4 |
| β-strand | 354-358 | 5 | 4 |
| α-helix | 365-383 | 19 | |
| α-helix | 384-386 | 3 | |
| α-helix | 389-391 | 3 | |
| α-helix | 399-412 | 14 | |
| α-helix | 414-419 | 6 | |
| α-helix | 431-445 | 15 | |
| α-helix | 448-464 | 17 | |
| 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 | 512-561 | 20 | |
| α-helix | 568-570 | 3 | |
| α-helix | 577-587 | 11 | |
| α-helix | 595-603 | 9 | |
| α-helix | 611-616 | 6 | |
| α-helix | 618-626 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 334 | 1 | |
| β-strand | 335 | 1 | 5 |
| α-helix | 336 | 1 | |
| α-helix | 339-342 | 4 | |
| α-helix | 347-348 | 2 | |
| β-strand | 349 | 1 | 6 |
| α-helix | 350-352 | 3 | |
| β-strand | 354-358 | 5 | 6 |
| β-strand | 361-362 | 2 | 5 |
| α-helix | 365-369 | 5 | |
| β-strand | 376-379 | 4 | 6 |
| α-helix | 387-389 | 3 | |
| β-strand | 391-392 | 2 | 5 |
| β-strand | 394-403 | 10 | 6 |
| α-helix | 405-409 | 5 | |
| α-helix | 417-421 | 5 | |
| β-strand | 432-437 | 6 | 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 |
| α-helix | 521-522 | 2 | |
| β-strand | 524-525 | 2 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Angiotensin-converting enzyme | A | protein | 596 | Ovis aries | A0A6P3TFC0 (AlphaFold model) |
| RaTG13 rbd | E | protein | 195 | Bat coronavirus RaTG13 | A0ABF7PLN6 |
>9KOS_1 Angiotensin-converting enzyme (chains A) STTEGQAKTFLEKFNHEAEDLSYQSSLASWNYNTNITDENVQKMNEARAKWSAFYEEQSR MARTYSLEEIQNLTLKRQLKALQHSGTSVLSAEKSKRLNTILNKMSTIYSTGKVLDPNTQ ECLALEPGLDDIMENSRDYNRRLWAWEGWRAEVGKQLRPLYEEYVVLENEMARANNYEDY GDYWRGDYEVTGAGDYDYSRDQLMKDVERTFEEIKPLYEQLHAYVRAKLMDTYPSYISPT GCLPAHLLGDMWGRFWTNLYSLTVPFEHKPSIDVTEKMKNQSWDAERIFKEAEKFFVSIG LPYMTQGFWDNSMLTEPGDGRKVVCHPTAWDLGKGDFRIKMCTKVTMDDFLTAHHEMGHI QYDMAYATQPYLLRNGANEGFHEAVGEIMSLSAATPHYLKALGLLAPDFYEDNETEINFL LKQALTIVGTLPFTYMLEKWRWMVFKGEIPKQQWMEKWWEMKREIVGVVEPLPHDETYCD PACLFHVAEDYSFIRYYTRTIYQFQFHEALCKTAKHEGALFKCDISNSTEAGQRLLQMLR LGKSEPWTLALENIVGIKTMDVKPLLNYFEPLFTWLKEQNRNSFVGWSTEWTPYSD
>9KOS_2 RaTG13 RBD (chains E) TNLCPFGEVFNATTFASVYAWNRKRISNCVADYSVLYNSTSFSTFKCYGVSPTKLNDLCF TNVYADSFVITGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNSKHIDAKEGGNFNYL YRLFRKANLKPFERDISTEIYQAGSKPCNGQTGLNCYYPLYRYGFYPTDGVGHQPYRVVV LSFELLNAPATVCGH
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 1 |
Crystal structure of RaTG13 RBD complexed with sheep ACE2. Lan, J., Wang, C.H. To be published.
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