Cryo-EM structure of P.nat ACE2 mutant in complex with MOW15-22 RBD. Determined by electron microscopy at 3.31 Å resolution. Released 12 Feb 2025.
Explore 8ZUF in 3D Show helices and sheets RCSB PDB PDBe
8ZUF contains 46 α-helices and 20 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 | 24-52 | 29 | |
| α-helix | 57-80 | 24 | |
| α-helix | 81-83 | 3 | |
| α-helix | 86-88 | 3 | |
| α-helix | 92-102 | 11 | |
| α-helix | 105-108 | 4 | |
| α-helix | 111-129 | 19 | |
| β-strand | 132-135 | 4 | 1 |
| β-strand | 138-144 | 7 | 1 |
| α-helix | 145-152 | 8 | |
| α-helix | 158-168 | 11 | |
| α-helix | 169-173 | 5 | |
| α-helix | 174-192 | 19 | |
| α-helix | 199-203 | 5 | |
| 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 | 294-299 | 6 | |
| α-helix | 304-316 | 13 | |
| α-helix | 321-324 | 4 | |
| 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 | 390-392 | 3 | |
| α-helix | 400-412 | 13 | |
| α-helix | 415-420 | 6 | |
| α-helix | 432-446 | 15 | |
| α-helix | 449-465 | 17 | |
| 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 | 513-532 | 20 | |
| α-helix | 539-541 | 3 | |
| α-helix | 548-558 | 11 | |
| α-helix | 566-574 | 9 | |
| α-helix | 582-587 | 6 | |
| α-helix | 589-599 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 396-398 | 3 | |
| β-strand | 400-402 | 3 | 5 |
| α-helix | 411-414 | 4 | |
| β-strand | 419-424 | 6 | 5 |
| β-strand | 442-447 | 6 | 5 |
| α-helix | 453-456 | 4 | |
| α-helix | 464-468 | 5 | |
| β-strand | 479-484 | 6 | 5 |
| β-strand | 497-508 | 12 | 6 |
| β-strand | 518-525 | 8 | 6 |
| α-helix | 533-535 | 3 | |
| α-helix | 536-548 | 13 | |
| β-strand | 552-557 | 6 | 6 |
| β-strand | 562 | 1 | 7 |
| α-helix | 567 | 1 | |
| β-strand | 568 | 1 | 7 |
| α-helix | 569 | 1 | |
| β-strand | 570-578 | 9 | 6 |
| β-strand | 586-593 | 8 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Angiotensin-converting enzyme | A | protein | 782 | Pipistrellus nathusii | Q56H28 (AlphaFold model) |
| MOW15-22 rbd | B | protein | 213 | Middle East respiratory syndrome-related coronavirus | A3EXD0 (AlphaFold model) |
>8ZUF_1 Angiotensin-converting enzyme (chains A) EEKAREFLDKFNSEAENWSHESALASWDYNTNINDKNAQKMNEADSKWSAFYKEHSKLAQ GFPLQEIQNSTIKLQLQILQQNGSSVLTAEKSKRLSTILTTMSTIYSTGKVCNPNNPQQC FTLSGLEDIMEKSKDYHQRLWIWEGWRSEVGKQLRPLYEEYVALKNEMARGNNYKDYGDY WRGDYETEGGDGYNYSRNHLIEDVDRIFLEIKPLYEQLHAYVRAKLMNAYPSRISPTGCL PAHLLGDMWGRFWTNLYNLTVPFEKKQNIDVTDTMKKQSWDAEKIFKEAEKFYLSVGLHN MTPEFWNNSMLTEPSDGRQVVCHPTAWDLGKNDFRIKMCTKVTMDDFLTAHHEMGHIQYD MAYAKQPYLLRNGANEGFHEAVGEIMSLSAATPKHLKDLGLLAQNYPEDYETEINFLLKQ ALNIVGTLPFTYMLEKWRWMVFEGKIPKEQWMEKWWEMKREIVGVVEPLPHDETYCDPAS LFHVANDYSFIRYFTRTILEFQFQEALCQIANHTGPLHKCDISNSTEAGKQLKNMLELGK SKPWTFALEQIARTKEMDAKPLLNYFKPLFSWLKELNGNSVGWSADWSPYSEQSIKVRIS LKSALGEKAYEWNDNEMYLFRSSVAYAMRVYFLKVKNETIPFRAEDVWVSDEKIRVSFKF FVTSPTNVSDIIPRSEVEDAIRMSRGRINDAFRLDDKTLEFLGIQPTLGPPYQPPVTIWL IVFGVVMGMVVIGIGVLIFTGIRDRKKKNQAENEENPYSSVNLSKGENNPGFQSGDDVQT SF
>8ZUF_2 MOW15-22 RBD (chains B) ECDFTKLFIGQVPQPYEFGRLVFTNCNYNFTKLLSYFQVNTFQCQKVTPESIATGCYSSL TVDWFAYRVEDKSDLLPGSSSDLQRFNYKPTYSNPTCLISAYTNLVPLGGVNPTNYTTLT NCYGCVDKDPANPWGDQICIPEFVTEVEPGFRPKPSCARVGLEGHISGNDTYSAIVTNGE LDSTGDPIWRKGVALTKQPIDSSRADLAFFVSV
Multiple independent acquisitions of ACE2 usage in MERS-related coronaviruses. Ma, C.B., Liu, C., Park, Y.J. et al. Cell (2025) 188:1693. DOI 10.1016/j.cell.2024.12.031 · PubMed
Other PDB entries of the same protein (UniProt Q56H28 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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