Cryo-EM structure of cat ACE2 and SARS-CoV-2 RBD. Determined by electron microscopy at 3.0 Å resolution. Released 2 Sept 2020.
Explore 7C8D in 3D Show helices and sheets RCSB PDB PDBe
7C8D contains 42 α-helices and 23 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 | 21-52 | 32 | |
| α-helix | 57-80 | 24 | |
| α-helix | 85-87 | 3 | |
| α-helix | 91-101 | 11 | |
| α-helix | 110-127 | 18 | |
| β-strand | 131-133 | 3 | 1 |
| β-strand | 141-143 | 3 | 1 |
| α-helix | 144-148 | 5 | |
| α-helix | 149-154 | 6 | |
| α-helix | 158-170 | 13 | |
| α-helix | 177-193 | 17 | |
| α-helix | 199-204 | 6 | |
| β-strand | 209 | 1 | 2 |
| β-strand | 217 | 1 | 2 |
| α-helix | 221-251 | 31 | |
| β-strand | 262-263 | 2 | 3 |
| α-helix | 276-278 | 3 | |
| α-helix | 279-282 | 4 | |
| α-helix | 289-290 | 2 | |
| α-helix | 294-299 | 6 | |
| α-helix | 304-317 | 14 | |
| α-helix | 320-324 | 5 | |
| α-helix | 327-330 | 4 | |
| β-strand | 348-350 | 3 | 4 |
| β-strand | 356-358 | 3 | 4 |
| α-helix | 367-384 | 18 | |
| α-helix | 385-387 | 3 | |
| α-helix | 390-392 | 3 | |
| α-helix | 401-412 | 12 | |
| α-helix | 415-418 | 4 | |
| α-helix | 434-446 | 13 | |
| α-helix | 447-449 | 3 | |
| α-helix | 450-465 | 16 | |
| 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 | 514-532 | 19 | |
| α-helix | 548-558 | 11 | |
| α-helix | 561-563 | 3 | |
| α-helix | 566-574 | 9 | |
| α-helix | 582-587 | 6 | |
| α-helix | 589-598 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 339-342 | 4 | |
| β-strand | 349 | 1 | 5 |
| α-helix | 353 | 1 | |
| β-strand | 354-358 | 5 | 5 |
| α-helix | 366-369 | 4 | |
| β-strand | 376-380 | 5 | 5 |
| β-strand | 391-392 | 2 | 6 |
| β-strand | 394-403 | 10 | 5 |
| α-helix | 404-409 | 6 | |
| α-helix | 417 | 1 | |
| α-helix | 418-422 | 5 | |
| β-strand | 431-437 | 7 | 5 |
| β-strand | 448 | 1 | 7 |
| β-strand | 452-454 | 3 | 8 |
| 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 |
| β-strand | 507-516 | 10 | 5 |
| β-strand | 524-525 | 2 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Angiotensin-converting enzyme 2 | A | protein | 732 | Felis catus | Q56H28 (AlphaFold model) |
| Spike protein S1 | B | protein | 195 | Severe acute respiratory syndrome coronavirus 2 | P0DTC2 (AlphaFold model) |
>7C8D_1 Angiotensin-converting enzyme 2 (chains A) MQSTTEELAKTFLEKFNHEAEELSYQSSLASWNYNTNITDENVQKMNEAGAKWSAFYEEQ SKLAKTYPLAEIHNTTVKRQLQALQQSGSSVLSADKSQRLNTILNAMSTIYSTGKACNPN NPQECLLLEPGLDDIMENSKDYNERLWAWEGWRAEVGKQLRPLYEEYVALKNEMARANNY EDYGDYWRGDYEEEWTDGYNYSRSQLIKDVEHTFTQIKPLYQHLHAYVRAKLMDTYPSRI SPTGCLPAHLLGDMWGRFWTNLYPLTVPFGQKPNIDVTDAMVNQSWDARRIFKEAEKFFV SVGLPNMTQGFWENSMLTEPGDSRKVVCHPTAWDLGKGDFRIKMCTKVTMDDFLTAHHEM GHIQYDMAYAVQPFLLRNGANEGFHEAVGEIMSLSAATPNHLKTIGLLSPGFSEDSETEI NFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKEQWMQKWWEMKREIVGVVEPVPHDET YCDPASLFHVANDYSFIRYYTRTIYQFQFQEALCRIAKHEGPLHKCDISNSSEAGKKLLQ MLTLGKSKPWTLALEHVVGEKKMNVTPLLKYFEPLFTWLKEQNRNSFVGWNTDWRPYADQ SIKVRISLKSALGDEAYEWNDNEMYLFRSSVAYAMREYFSKVKNQTIPFVEDNVWVSNLK PRISFNFFVTASKNVSDVIPRSEVEEAIRMSRSRINDAFRLDDNSLEFLGIQPTLSPPYQ PPVTHHHHHHHH
>7C8D_2 Spike protein S1 (chains B) TNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCF TNVYADSFVIRGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYL YRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFPLQSYGFQPTNGVGYQPYRVVV LSFELLHAPATVCGP
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 1 |
Broad host range of SARS-CoV-2 and the molecular basis for SARS-CoV-2 binding to cat ACE2. Wu, L., Chen, Q., Liu, K. et al. Cell Discov (2020) 6:68-68. DOI 10.1038/s41421-020-00210-9 · 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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