Structure of the prefusion HKU5-19s Spike trimer (conformation 1). Determined by electron microscopy at 2.0 Å resolution. Released 26 Feb 2025.
Explore 9EA0 in 3D Show helices and sheets RCSB PDB PDBe
9EA0 contains 156 α-helices and 237 β-strands across 3 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 | 29-30 | 2 | |
| α-helix | 34-36 | 3 | |
| β-strand | 37-39 | 3 | 1 |
| α-helix | 41-43 | 3 | |
| α-helix | 57-59 | 3 | |
| α-helix | 63 | 1 | |
| β-strand | 64 | 1 | 2 |
| α-helix | 65-66 | 2 | |
| β-strand | 74-82 | 9 | 3 |
| α-helix | 83-84 | 2 | |
| β-strand | 90-92 | 3 | 4 |
| β-strand | 95-96 | 2 | 5 |
| α-helix | 97-98 | 2 | |
| β-strand | 99-100 | 2 | 6 |
| β-strand | 103-104 | 2 | 6 |
| β-strand | 107-109 | 3 | 1 |
| β-strand | 117-118 | 2 | 7 |
| β-strand | 123-127 | 5 | 4 |
| β-strand | 134-136 | 3 | 8 |
| β-strand | 144-146 | 3 | 8 |
| β-strand | 147-148 | 2 | 9 |
| β-strand | 154-157 | 4 | 7 |
| β-strand | 159-163 | 5 | 10 |
| β-strand | 168-173 | 6 | 10 |
| β-strand | 175-182 | 8 | 7 |
| β-strand | 187-197 | 11 | 7 |
| β-strand | 214-216 | 3 | 5 |
| α-helix | 232-240 | 9 | |
| β-strand | 241-244 | 4 | 7 |
| β-strand | 249-253 | 5 | 7 |
| β-strand | 261-267 | 7 | 4 |
| β-strand | 272-276 | 5 | 4 |
| β-strand | 287 | 1 | 2 |
| β-strand | 288-293 | 6 | 4 |
| α-helix | 298-299 | 2 | |
| β-strand | 301-304 | 4 | 7 |
| β-strand | 307-309 | 3 | 5 |
| β-strand | 318-319 | 2 | 9 |
| β-strand | 322-326 | 5 | 4 |
| β-strand | 328-336 | 9 | 3 |
| β-strand | 342-347 | 6 | 3 |
| α-helix | 352-360 | 9 | |
| β-strand | 368-371 | 4 | 11 |
| β-strand | 381-385 | 5 | 12 |
| β-strand | 390-391 | 2 | 13 |
| α-helix | 395-398 | 4 | |
| β-strand | 400 | 1 | 14 |
| α-helix | 401-404 | 4 | |
| α-helix | 405-407 | 3 | |
| β-strand | 409-413 | 5 | 15 |
| β-strand | 416-418 | 3 | 13 |
| α-helix | 420-425 | 6 | |
| β-strand | 428-435 | 8 | 15 |
| α-helix | 441-443 | 3 | |
| β-strand | 447 | 1 | 13 |
| β-strand | 449-456 | 8 | 15 |
| α-helix | 459-465 | 7 | |
| α-helix | 472 | 1 | |
| α-helix | 473-477 | 5 | |
| β-strand | 486-492 | 7 | 15 |
| β-strand | 500 | 1 | 14 |
| α-helix | 501-503 | 3 | |
| β-strand | 505-515 | 11 | 16 |
| β-strand | 520-522 | 3 | 16 |
| α-helix | 525-526 | 2 | |
| α-helix | 534-537 | 4 | |
| β-strand | 546-549 | 4 | 16 |
| β-strand | 553-561 | 9 | 16 |
| β-strand | 567-575 | 9 | 15 |
| β-strand | 583-585 | 3 | 13 |
| α-helix | 586-588 | 3 | |
| β-strand | 603-607 | 5 | 12 |
| β-strand | 610-614 | 5 | 12 |
| β-strand | 615-619 | 5 | 17 |
| β-strand | 629-631 | 3 | 17 |
| β-strand | 637-641 | 5 | 17 |
| β-strand | 647-651 | 5 | 17 |
| β-strand | 659-663 | 5 | 11 |
| β-strand | 668-674 | 7 | 11 |
| α-helix | 678-683 | 6 | |
| α-helix | 690-698 | 9 | |
| β-strand | 705-707 | 3 | 11 |
| β-strand | 710-713 | 4 | 11 |
| β-strand | 715-722 | 8 | 18 |
| β-strand | 728 | 1 | 18 |
| β-strand | 733-736 | 4 | 18 |
| α-helix | 737-739 | 3 | |
| β-strand | 755-760 | 6 | 18 |
| β-strand | 767 | 1 | 19 |
| α-helix | 769-771 | 3 | |
| β-strand | 776-794 | 19 | 20 |
| β-strand | 800-802 | 3 | 21 |
| α-helix | 804-809 | 6 | |
| α-helix | 813-819 | 7 | |
| α-helix | 820-822 | 3 | |
| α-helix | 825-848 | 24 | |
| α-helix | 849-853 | 5 | |
| β-strand | 856 | 1 | 22 |
| α-helix | 858-860 | 3 | |
| β-strand | 863-864 | 2 | 23 |
| β-strand | 867-868 | 2 | 23 |
| α-helix | 874-876 | 3 | |
| α-helix | 881-883 | 3 | |
| α-helix | 887-894 | 8 | |
| α-helix | 906-913 | 8 | |
| α-helix | 917-919 | 3 | |
| α-helix | 920-923 | 4 | |
| α-helix | 925-929 | 5 | |
| β-strand | 930-932 | 3 | 21 |
| α-helix | 933-935 | 3 | |
| α-helix | 939-950 | 12 | |
| β-strand | 965-966 | 2 | 24 |
| α-helix | 970-979 | 10 | |
| α-helix | 985-990 | 6 | |
| α-helix | 992-1005 | 14 | |
| α-helix | 1006-1008 | 3 | |
| α-helix | 1015-1036 | 22 | |
| α-helix | 1037-1039 | 3 | |
| α-helix | 1049-1055 | 7 | |
| α-helix | 1058-1100 | 43 | |
| α-helix | 1101-1105 | 5 | |
| β-strand | 1119-1128 | 10 | 20 |
| β-strand | 1131-1150 | 20 | 20 |
| β-strand | 1153-1154 | 2 | 25 |
| β-strand | 1162-1165 | 4 | 25 |
| β-strand | 1168-1172 | 5 | 20 |
| β-strand | 1186-1190 | 5 | 20 |
| β-strand | 1193-1197 | 5 | 20 |
| β-strand | 1204-1207 | 4 | 25 |
| β-strand | 1214-1215 | 2 | 25 |
| α-helix | 1222-1224 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Spike glycoprotein | A, B, C | protein | 1365 | Pipistrellus bat coronavirus HKU5 | A3EXD0 (AlphaFold model) |
>9EA0_1 Spike glycoprotein (chains A, B, C) MGILPSPGMPALLSLVSLLSVLLMGCVAETGTQSVDMGTTGSGNCIESQVQPDFFETARN TWPLSIDTSKAEGVIYPNGKSYSNITLTYTGLYPKANDLGKQYVFSDGHSSPGTLSRLFV SNYSRQVEPFDSGFVVRIGAAANKTGTTIISQSTNRPIKKIYPAFMLGHSVGNYTPTNIT GRYLNHTLVILPDGCGTLVHAFYCILQPRTQAYCAGASTFTSVTVWDTPASDCANSQSYN RLANLNAFKLYFDLINCTFRYNYTITEDENAEWFGITQDTQGVHLYSSRKENVFRNNMFH FATLPVYQKILYYTVIPRSIRSPFNDRKAWAAFYIYKLHPLTYLLNFDVEGYITKAVDCG YDDLAQLQCSYQSFDVETGVYSVSSFEASPRGEFIEQATTQECDFTPMLTGTPPPIYNFK RLVFTNCNYNLTKLLSLFQVSEFSCHQVSPSSLATGCYSSLTVDYFAYSTDMSSYLQPGS AGEIVQFNYKQDFSNPTCRVLATVPQNLTTITKPSNYAYLTECYKTSAYGKNYLYNAPGG YTPCLSLASRGFSTKYQSHSDGELTTTGYIYPVTGNLQMAFIISVQYGTDTNSVCPMQAL RNDTSIEDKLDVCVEYSLHGITGRGVFHNCTSVGLRNQRFVYDTFDNLVGYHSYNGNYYC VRPCVSVPVSVIYDKVSNSHATLFGSVACSHVTTMMSQFSRMTKTNLLARTTPGPLQTVV GCAMGFINTSMVVDECQLPLGQSLCAIPPNPSARLARASSGVTDVFQIATLNFTSPLTLA PINSTGFVVAVPTNFTFGVTQEYIETTIQKITVDCKQYVCNGFKKCEELLTEYGQFCSKI NQALHGANLRQDESIANLFSSIKTQNTQPLQAGLNGDFNLTMLQIPQVTTGERKYRSAIE DLLFNKVTIADPGYMQGYDECMQQGPQSARDLICAQYVAGYKVLPPLYDPYMEAAYTSSL LGSIAGASWTAGLSSFAAIPFAQSIFYRLNGVGITQQVLSENQKIIANKFNQALGAMQTG FTTTNLAFNKVQDAVNANAMALSKLAAELSNTFGAISSSISDILARLDPPEQEAQIDRLI NGRLTSLNAFVAQQLVRTEAAARSAQLAQDKVNECVKSQSKRNGFCGTGTHIVSFAINAP NGLYFFHVGYQPTSHVNATAAYGLCNTENPPKCIAPIGGYFVLNQTTSTVANSEQQWYYT GSSFFHPEPITEVNSKYVSMDVKFENLTNKLPPPLLSNTTDLDFKEELEEFFKNVSSQGP NFQEISKINTTLLNLNTELMVLSEVVKQLNESYIDLKELGNYTFYQKGSGYIPEAPRDGQ AYVRKDGEWVLLSTFLGGSGLNDIFEAQKIEWHEGGSHHHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 9 |
| FOL | Folic acid | C19 H19 N7 O6 | 3 |
| ZN | Zinc ion | Zn | 6 |
| EIC | Linoleic acid | C18 H32 O2 | 3 |
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 A3EXD0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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