Structure of the prefusion HKU5-19s Spike trimer (conformation 2). Determined by electron microscopy at 2.0 Å resolution. Released 26 Feb 2025.
Explore 9EH8 in 3D Show helices and sheets RCSB PDB PDBe
9EH8 contains 156 α-helices and 240 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 | 47-49 | 3 | |
| α-helix | 57-59 | 3 | |
| α-helix | 63 | 1 | |
| β-strand | 64 | 1 | 2 |
| α-helix | 65-66 | 2 | |
| β-strand | 70-71 | 2 | 3 |
| β-strand | 75-82 | 8 | 4 |
| α-helix | 83-84 | 2 | |
| β-strand | 90-92 | 3 | 5 |
| β-strand | 95-96 | 2 | 6 |
| α-helix | 97-98 | 2 | |
| β-strand | 99-100 | 2 | 7 |
| β-strand | 103-104 | 2 | 7 |
| β-strand | 107-109 | 3 | 1 |
| α-helix | 112-114 | 3 | |
| β-strand | 117-118 | 2 | 8 |
| β-strand | 123-127 | 5 | 5 |
| β-strand | 134-137 | 4 | 9 |
| β-strand | 140-146 | 7 | 9 |
| β-strand | 147-148 | 2 | 10 |
| β-strand | 154-157 | 4 | 8 |
| β-strand | 160-163 | 4 | 11 |
| β-strand | 168-172 | 5 | 11 |
| β-strand | 175-182 | 8 | 8 |
| β-strand | 187-197 | 11 | 8 |
| β-strand | 214 | 1 | 12 |
| α-helix | 232-240 | 9 | |
| β-strand | 241-244 | 4 | 8 |
| β-strand | 249-253 | 5 | 8 |
| β-strand | 261-268 | 8 | 5 |
| β-strand | 271-276 | 6 | 5 |
| β-strand | 287 | 1 | 2 |
| β-strand | 288-293 | 6 | 5 |
| α-helix | 298-299 | 2 | |
| β-strand | 301-304 | 4 | 8 |
| β-strand | 307 | 1 | 12 |
| β-strand | 308-309 | 2 | 6 |
| β-strand | 318-319 | 2 | 10 |
| β-strand | 322-326 | 5 | 5 |
| β-strand | 328-336 | 9 | 4 |
| β-strand | 342-347 | 6 | 4 |
| α-helix | 352-360 | 9 | |
| β-strand | 368-372 | 5 | 13 |
| α-helix | 373-376 | 4 | |
| β-strand | 382-385 | 4 | 14 |
| β-strand | 390-391 | 2 | 15 |
| α-helix | 395-398 | 4 | |
| β-strand | 399-400 | 2 | 16 |
| α-helix | 402-404 | 3 | |
| α-helix | 405-407 | 3 | |
| β-strand | 409-413 | 5 | 17 |
| β-strand | 416-418 | 3 | 15 |
| α-helix | 420-424 | 5 | |
| β-strand | 428-435 | 8 | 17 |
| α-helix | 439-444 | 6 | |
| β-strand | 447 | 1 | 15 |
| β-strand | 449-456 | 8 | 17 |
| α-helix | 459-465 | 7 | |
| α-helix | 472-476 | 5 | |
| β-strand | 486-492 | 7 | 17 |
| β-strand | 499-500 | 2 | 16 |
| β-strand | 505-514 | 10 | 18 |
| β-strand | 521-522 | 2 | 18 |
| α-helix | 524-526 | 3 | |
| α-helix | 534-537 | 4 | |
| β-strand | 546-549 | 4 | 18 |
| β-strand | 553-561 | 9 | 18 |
| β-strand | 567-575 | 9 | 17 |
| β-strand | 583-585 | 3 | 15 |
| α-helix | 586-588 | 3 | |
| β-strand | 602-607 | 6 | 14 |
| β-strand | 610-619 | 10 | 14 |
| α-helix | 625-627 | 3 | |
| β-strand | 629-631 | 3 | 14 |
| β-strand | 637-641 | 5 | 14 |
| β-strand | 647-651 | 5 | 14 |
| β-strand | 658-663 | 6 | 13 |
| β-strand | 668-674 | 7 | 13 |
| α-helix | 678-686 | 9 | |
| α-helix | 702-704 | 3 | |
| β-strand | 705-707 | 3 | 13 |
| β-strand | 710-713 | 4 | 13 |
| β-strand | 715-722 | 8 | 19 |
| β-strand | 727-730 | 4 | 19 |
| β-strand | 733-736 | 4 | 19 |
| α-helix | 737-739 | 3 | |
| β-strand | 755-760 | 6 | 19 |
| β-strand | 767 | 1 | 20 |
| α-helix | 769-771 | 3 | |
| β-strand | 776-794 | 19 | 21 |
| β-strand | 800-802 | 3 | 22 |
| α-helix | 804-809 | 6 | |
| α-helix | 813-819 | 7 | |
| α-helix | 820-822 | 3 | |
| α-helix | 823-848 | 26 | |
| α-helix | 849-853 | 5 | |
| β-strand | 856 | 1 | 23 |
| α-helix | 858-860 | 3 | |
| β-strand | 863-864 | 2 | 24 |
| β-strand | 867-868 | 2 | 24 |
| α-helix | 870-872 | 3 | |
| α-helix | 881-883 | 3 | |
| α-helix | 887-894 | 8 | |
| α-helix | 906-911 | 6 | |
| α-helix | 925-928 | 4 | |
| β-strand | 930-932 | 3 | 22 |
| α-helix | 933-935 | 3 | |
| α-helix | 939-950 | 12 | |
| β-strand | 965-966 | 2 | 25 |
| α-helix | 970-980 | 11 | |
| α-helix | 985-990 | 6 | |
| α-helix | 992-1004 | 13 | |
| α-helix | 1007-1009 | 3 | |
| α-helix | 1015-1036 | 22 | |
| α-helix | 1037-1039 | 3 | |
| α-helix | 1049-1055 | 7 | |
| α-helix | 1060-1100 | 41 | |
| α-helix | 1101-1105 | 5 | |
| β-strand | 1119-1128 | 10 | 21 |
| β-strand | 1131-1150 | 20 | 21 |
| β-strand | 1153-1154 | 2 | 26 |
| β-strand | 1162-1165 | 4 | 26 |
| β-strand | 1168-1172 | 5 | 21 |
| β-strand | 1186-1190 | 5 | 21 |
| β-strand | 1193-1197 | 5 | 21 |
| β-strand | 1204-1207 | 4 | 26 |
| β-strand | 1214-1215 | 2 | 26 |
| 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) |
>9EH8_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 |
|---|---|---|---|
| EIC | Linoleic acid | C18 H32 O2 | 3 |
| FOL | Folic acid | C19 H19 N7 O6 | 3 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 15 |
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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