Structure of angiotensin II type 1 receptor bound to a b-arrestin biased allosteric modulator stabilized by a synthetic nanobody. Determined by electron microscopy at 3.02 Å resolution. Released 26 Aug 2026.
Explore 9Q0F in 3D Show helices and sheets RCSB PDB PDBe
9Q0F contains 14 α-helices and 17 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 |
|---|---|---|---|
| β-strand | 12-14 | 3 | 1 |
| α-helix | 25-57 | 33 | |
| α-helix | 62-78 | 17 | |
| α-helix | 81-89 | 9 | |
| α-helix | 98-131 | 34 | |
| α-helix | 142-159 | 18 | |
| α-helix | 161-166 | 6 | |
| β-strand | 168-172 | 5 | 1 |
| β-strand | 177-181 | 5 | 1 |
| β-strand | 184 | 1 | 2 |
| α-helix | 193-200 | 8 | |
| α-helix | 201-205 | 5 | |
| α-helix | 206-228 | 23 | |
| α-helix | 238-268 | 31 | |
| α-helix | 274-296 | 23 | |
| α-helix | 298-303 | 6 | |
| α-helix | 308-316 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 3 |
| β-strand | 10-13 | 4 | 4 |
| β-strand | 17-25 | 9 | 3 |
| β-strand | 31-39 | 9 | 4 |
| β-strand | 46-52 | 7 | 4 |
| β-strand | 57-59 | 3 | 4 |
| β-strand | 64 | 1 | 3 |
| β-strand | 67-72 | 6 | 3 |
| β-strand | 77-83 | 7 | 3 |
| α-helix | 87-89 | 3 | |
| β-strand | 91-99 | 9 | 4 |
| β-strand | 114-116 | 3 | 4 |
| β-strand | 120-125 | 6 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Type-1 angiotensin II receptor | A | protein | 366 | Homo sapiens | P30556 (AlphaFold model) |
| TRV023 | B | protein | 8 | synthetic construct | |
| Nanobody NB.AT110i1 | D | protein | 134 | synthetic construct |
>9Q0F_1 Type-1 angiotensin II receptor (chains A) DYKDDDDKILNSSTEDGIKRIQDDCPKAGRHNYIFVMIPTLYSIIFVVGIFGNSLVVIVI YFYMKLKTVASVFLLNLALADLCFLLTLPLWAVYTAMEYRWPFGNYLCKIASASVSFNLY ASVFLLTCLSIDRYLAIVHPMKSRLRRTMLVAKVTCIIIWLLAGLASLPAIIHRNVFFIE NTNITVCAFHYESQNSTLPIGLGLTKNILGFLFPFLIILTSYTLIWKALKKAYEIQKNKP RNDDIFKIIMAIVLFFFFSWIPHQIFTFLDVLIQLGIIRDCRIADIVDTAMPITICIAYF NNCLNPLFYGFLGKKFKRYFLQLLKYIPPKAKSHSNLSTKMSTLSYRPSDNVSSSTKKPA PCFEVE
>9Q0F_2 TRV023 (chains B) GRVYKHPA
>9Q0F_3 Nanobody NB.AT110i1 (chains D) QVQLQESGGGLVQAGGSLRLSCAASGNIFDVDIMGWYRQAPGKERELVASITDGGSTDYA DSVKGRFTISRDNAKNTVYLQMNSLKPEDTAVYYCAAVAYPDIPTYFDYDSDNFYWGQGT QVTVSSLEHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1CNF | (7P)-N-[(1R)-3-amino-1-(6-methoxypyridin-3-yl)-3-oxopropyl]-7-(3-chlorophenyl)-… | C35 H33 Cl F3 N7 O3 | 1 |
| CLR | Cholesterol | C27 H46 O | 2 |
Conformational Basis of Functionally Selective Allosteric Modulation of the Angiotensin II type 1 Receptor by Small Molecules. Liu, S., Xiao, P., Elgeti, M. et al. To be published.
Other PDB entries of the same protein (UniProt P30556 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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