9RVT: ACE2 extracellular domain
ACE2 extracellular domain in complex with the macrocyclic peptide GR1.4. Determined by X-ray diffraction at 2.39 Å resolution. Released 8 Apr 2026.
- Method
- X-ray diffraction
- Resolution
- 2.39 Å
- Organisms
- Homo sapiens, synthetic construct
- Chains
- 8
- Atoms
- 20,476
- Mol. weight
- 288.3 kDa
- Released
- 8 Apr 2026
Explore 9RVT in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9RVT contains 156 α-helices and 51 β-strands across 8 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.
Chain A: 39 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 21-52 | 32 | |
| α-helix | 56-80 | 25 | |
| α-helix | 91-102 | 12 | |
| α-helix | 110-129 | 20 | |
| β-strand | 132-133 | 2 | 1 |
| β-strand | 141-142 | 2 | 1 |
| α-helix | 144-148 | 5 | |
| α-helix | 149-154 | 6 | |
| α-helix | 158-167 | 10 | |
| α-helix | 168-172 | 5 | |
| α-helix | 173-193 | 21 | |
| α-helix | 199-203 | 5 | |
| α-helix | 204-207 | 4 | |
| β-strand | 209 | 1 | 2 |
| β-strand | 217 | 1 | 2 |
| α-helix | 219-251 | 33 | |
| β-strand | 260 | 1 | 3 |
| α-helix | 261 | 1 | |
| β-strand | 262-263 | 2 | 4 |
| 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 | 325-330 | 6 | |
| β-strand | 332 | 1 | 5 |
| β-strand | 347-352 | 6 | 5 |
| β-strand | 355-359 | 5 | 5 |
| α-helix | 366-384 | 19 | |
| α-helix | 385-387 | 3 | |
| 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 | 4 |
| α-helix | 499-502 | 4 | |
| α-helix | 504-507 | 4 | |
| α-helix | 514-532 | 19 | |
| α-helix | 539-541 | 3 | |
| α-helix | 548-558 | 11 | |
| α-helix | 566-574 | 9 | |
| α-helix | 582-587 | 6 | |
| α-helix | 589-598 | 10 | |
| α-helix | 599-601 | 3 | |
| β-strand | 607 | 1 | 3 |
Chain B: 38 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 21-52 | 32 | |
| α-helix | 58-80 | 23 | |
| α-helix | 85-87 | 3 | |
| α-helix | 91-102 | 12 | |
| α-helix | 110-129 | 20 | |
| β-strand | 131-133 | 3 | 6 |
| β-strand | 141-143 | 3 | 6 |
| α-helix | 144-148 | 5 | |
| α-helix | 149-154 | 6 | |
| α-helix | 158-167 | 10 | |
| α-helix | 168-172 | 5 | |
| α-helix | 173-193 | 21 | |
| α-helix | 199-204 | 6 | |
| β-strand | 209 | 1 | 7 |
| β-strand | 217 | 1 | 7 |
| α-helix | 219-251 | 33 | |
| β-strand | 260 | 1 | 8 |
| α-helix | 261 | 1 | |
| β-strand | 262-263 | 2 | 9 |
| α-helix | 276-278 | 3 | |
| α-helix | 279-282 | 4 | |
| α-helix | 294-299 | 6 | |
| α-helix | 304-317 | 14 | |
| α-helix | 320-324 | 5 | |
| α-helix | 327-330 | 4 | |
| β-strand | 332 | 1 | 10 |
| β-strand | 347-352 | 6 | 10 |
| β-strand | 355-359 | 5 | 10 |
| α-helix | 366-384 | 19 | |
| α-helix | 385-387 | 3 | |
| α-helix | 390-392 | 3 | |
| α-helix | 400-412 | 13 | |
| α-helix | 415-420 | 6 | |
| α-helix | 432-445 | 14 | |
| 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 | 9 |
| α-helix | 499-502 | 4 | |
| α-helix | 504-507 | 4 | |
| α-helix | 514-532 | 19 | |
| α-helix | 539-541 | 3 | |
| α-helix | 548-558 | 11 | |
| α-helix | 566-574 | 9 | |
| α-helix | 582-587 | 6 | |
| α-helix | 589-598 | 10 | |
| α-helix | 599-601 | 3 | |
| β-strand | 607 | 1 | 8 |
Chains C and E: 0 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 85-88 | 4 | 11 |
| β-strand | 91-93 | 3 | 11 |
Chain D: 40 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 21-52 | 32 | |
| α-helix | 56-80 | 25 | |
| α-helix | 91-105 | 15 | |
| α-helix | 110-129 | 20 | |
| β-strand | 131-133 | 3 | 12 |
| β-strand | 141-143 | 3 | 12 |
| α-helix | 144-148 | 5 | |
| α-helix | 149-154 | 6 | |
| α-helix | 158-167 | 10 | |
| α-helix | 168-173 | 6 | |
| α-helix | 174-193 | 20 | |
| α-helix | 199-204 | 6 | |
| α-helix | 205-207 | 3 | |
| β-strand | 209 | 1 | 13 |
| β-strand | 217 | 1 | 13 |
| α-helix | 219-251 | 33 | |
| β-strand | 260 | 1 | 14 |
| α-helix | 261 | 1 | |
| β-strand | 262-263 | 2 | 15 |
| α-helix | 264-266 | 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 | 325-330 | 6 | |
| β-strand | 332 | 1 | 16 |
| β-strand | 347-352 | 6 | 16 |
| β-strand | 355-359 | 5 | 16 |
| 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 | 450-465 | 16 | |
| α-helix | 470-472 | 3 | |
| α-helix | 473-480 | 8 | |
| α-helix | 481-485 | 5 | |
| β-strand | 487-488 | 2 | 15 |
| α-helix | 499-502 | 4 | |
| α-helix | 504-507 | 4 | |
| α-helix | 514-532 | 19 | |
| α-helix | 539-541 | 3 | |
| α-helix | 548-558 | 11 | |
| α-helix | 566-574 | 9 | |
| α-helix | 579-580 | 2 | |
| α-helix | 582-587 | 6 | |
| α-helix | 589-598 | 10 | |
| α-helix | 603-604 | 2 | |
| β-strand | 607 | 1 | 14 |
Chains F and H: 0 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 85-86 | 2 | 18 |
| β-strand | 92-93 | 2 | 18 |
Chain G: 39 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 21-52 | 32 | |
| α-helix | 56-80 | 25 | |
| α-helix | 85-87 | 3 | |
| α-helix | 91-101 | 11 | |
| α-helix | 110-129 | 20 | |
| β-strand | 132-134 | 3 | 19 |
| β-strand | 137-142 | 6 | 19 |
| α-helix | 144-148 | 5 | |
| α-helix | 149-154 | 6 | |
| α-helix | 158-168 | 11 | |
| α-helix | 169-173 | 5 | |
| α-helix | 174-192 | 19 | |
| α-helix | 199-204 | 6 | |
| β-strand | 209 | 1 | 20 |
| β-strand | 217 | 1 | 20 |
| α-helix | 219-251 | 33 | |
| β-strand | 260 | 1 | 21 |
| α-helix | 261 | 1 | |
| β-strand | 262-263 | 2 | 22 |
| α-helix | 264-266 | 3 | |
| α-helix | 276-278 | 3 | |
| α-helix | 279-282 | 4 | |
| α-helix | 289-290 | 2 | |
| α-helix | 294-298 | 5 | |
| α-helix | 304-317 | 14 | |
| α-helix | 320-324 | 5 | |
| α-helix | 325-328 | 4 | |
| β-strand | 347-350 | 4 | 23 |
| β-strand | 356-359 | 4 | 23 |
| α-helix | 366-384 | 19 | |
| α-helix | 385-387 | 3 | |
| 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 | 22 |
| 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 | 582-598 | 17 | |
| α-helix | 599-601 | 3 | |
| β-strand | 607 | 1 | 21 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Processed angiotensin-converting enzyme 2 | A, B, D, G | protein | 609 | Homo sapiens | Q9BYF1 (AlphaFold model) |
| macrocyclic peptide GR1.4 | C, E, F, H | protein | 14 | synthetic construct | |
Sequence of entity 1 (A, B, D, G), FASTA
>9RVT_1 Processed angiotensin-converting enzyme 2 (chains A, B, D, G)
GSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGDKWSAFLKEQS
TLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDN
PQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLYEEYVVLKNEMARANHYE
DYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYIS
PIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFKEAEKFFVS
VGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMG
HIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKSIGLLSPDFQEDNETEIN
FLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETY
CDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLFNM
LRLGKSEPWTLALENVVGAKNMNVRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPYADSS
PHHHHHHHH
Sequence of entity 2 (C, E, F, H), FASTA
>9RVT_2 macrocyclic peptide GR1.4 (chains C, E, F, H)
ACEPLGYNLFLCSG
Primary citation
Yeast Display Technology Enables Rapid Discovery of Low-Nanomolar Macrocyclic Peptide Inhibitors of Human Angiotensin-Converting Enzyme 2. Romanyuk, Z., Bettin, G., Brear, P. et al. J Med Chem (2026) 69:7689-7708. DOI 10.1021/acs.jmedchem.5c02876 · PubMed
Other PDB entries of the same protein (UniProt Q9BYF1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 9SPA 1.79 Å, Apo ACE2 extracellular domain
- 28KD 2.02 Å, ACE2 extracellular domain in complex with the macrocyclic peptide GR3.1.2
- 8BYJ 2.07 Å, The structures of Ace2 in complex with bicyclic peptide inhibitor
- 8B9P 2.11 Å, ACE2 in complex with bicyclic peptide inhibitor
- 8XSF 2.16 Å, SARS-CoV-2 rbd + imcas-364 + hACE2
- 1R42 2.2 Å, Native Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2)
- 7JVO 2.2 Å, Importin alpha bound to the C-terminus of ACE2
- 8TOR 2.2 Å, ACE2-peptide 2 complex
- 9RVA 2.2 Å, Crystal structure of the extracellular part of human ACE2 in complex with the…
- 9UE7 2.27 Å, Cryo-EM structure of SARS-CoV-2 KP.2 spike in complex with ACE2
- 8TOQ 2.3 Å, ACE2-peptide 1 complex
- 8BFW 2.33 Å, The structures of Ace2 in complex with bicyclic peptide inhibitor
Browse structure collections
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