Structure of nanobody AT206 in complex with the angiotensin II type I receptor (AT1R). Determined by electron microscopy at 3.2 Å resolution. Released 5 Mar 2025.
Explore 9EAJ in 3D Show helices and sheets RCSB PDB PDBe
9EAJ contains 22 α-helices and 35 β-strands across 4 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 | 31-51 | 21 | |
| α-helix | 52-56 | 5 | |
| α-helix | 62-89 | 28 | |
| α-helix | 98-131 | 34 | |
| α-helix | 143-159 | 17 | |
| α-helix | 161-166 | 6 | |
| β-strand | 167-171 | 5 | 1 |
| β-strand | 178-183 | 6 | 1 |
| α-helix | 191-201 | 11 | |
| α-helix | 205-243 | 39 | |
| α-helix | 248-267 | 20 | |
| α-helix | 283-305 | 23 | |
| α-helix | 309-322 | 14 | |
| α-helix | 323-327 | 5 | |
| α-helix | 328-1235 | 15 | |
| α-helix | 1237-1267 | 31 | |
| α-helix | 1278-1282 | 5 | |
| α-helix | 1284-1291 | 8 | |
| α-helix | 1294-1305 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 31 | 1 | |
| β-strand | 32 | 1 | 2 |
| β-strand | 33-37 | 5 | 3 |
| β-strand | 45-50 | 6 | 3 |
| β-strand | 56 | 1 | 3 |
| β-strand | 92 | 1 | 4 |
| β-strand | 93-94 | 2 | 3 |
| β-strand | 97 | 1 | 2 |
| β-strand | 108-109 | 2 | 1 |
| β-strand | 115 | 1 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-10 | 5 | 5 |
| β-strand | 14 | 1 | 6 |
| β-strand | 21-28 | 8 | 5 |
| α-helix | 32-34 | 3 | |
| β-strand | 36-42 | 7 | 7 |
| β-strand | 48-55 | 8 | 7 |
| β-strand | 61-63 | 3 | 7 |
| β-strand | 71-76 | 6 | 5 |
| β-strand | 81-86 | 6 | 5 |
| β-strand | 95-102 | 8 | 7 |
| α-helix | 108-111 | 4 | |
| β-strand | 116 | 1 | 7 |
| β-strand | 118 | 1 | 5 |
| β-strand | 121-123 | 3 | 7 |
| β-strand | 124 | 1 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-7 | 3 | 8 |
| β-strand | 11-14 | 4 | 9 |
| β-strand | 20-26 | 7 | 8 |
| β-strand | 34-39 | 6 | 9 |
| β-strand | 46-49 | 4 | 9 |
| β-strand | 55 | 1 | 9 |
| α-helix | 56 | 1 | |
| β-strand | 63-68 | 6 | 8 |
| β-strand | 71-76 | 6 | 8 |
| β-strand | 86-91 | 6 | 9 |
| α-helix | 95-97 | 3 | |
| β-strand | 99-100 | 2 | 9 |
| β-strand | 104-108 | 5 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nanobody AT206,Type-1 angiotensin II receptor,Soluble cytochrome b562 | A, B | protein | 583 | Camelidae, Homo sapiens, Escherichia coli | P30556 (AlphaFold model) |
| BAG2 Anti-BRIL Fab Heavy Chain | C | protein | 231 | synthetic construct | |
| BAG2 Anti-BRIL Fab Light Chain | D | protein | 215 | synthetic construct |
>9EAJ_1 Nanobody AT206,Type-1 angiotensin II receptor,Soluble cytochrome b562 (chains A, B) QVQLQESGGGLVQAGGSLRLSCAASGSISYYRMGWYRQAPGKEREFVAGIGVGTTTNYAD SVKGRFTISRDNAKNTVYLQMNSLKPEDTAVYYCAAYNYFPRSIVYYYVYWGQGTQVTVS SGGSGEDQVDPRLIDGKILNSSTEDGIKRIQDDCPKAGRHNYIFVMIPTLYSIIFVVGIF GNSLVVIVIYFYMKLKTVASVFLLNLALADLCFLLTLPLWAVYTAMEYRWPFGNYLCKIA SASVSFNLYASVFLLTCLSIDRYLAIVHPMKSRLRRTMLVAKVTCIIIWLLAGLASLPAI IHRNVFFIENTNITVCAFHYESQNSTLPIGLGLTKNILGFLFPFLIILTSYTLIWKALKK AYDLEDNWETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMK DFRHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKTTRNAYIQKYLERARSTLDKLNDD IFKIIMAIVLFFFFSWIPHQIFTFLDVLIQLGIIRDCRIADIVDTAMPITICIAYFNNCL NPLFYGFLGKKFKRYFLQLLKYGGSSLEVLFQGPTETSQVAPA
>9EAJ_2 BAG2 Anti-BRIL Fab Heavy Chain (chains C) EISEVQLVESGGGLVQPGGSLRLSCAASGFNVVDFSLHWVRQAPGKGLEWVAYISSSSGS TSYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARWGYWPGEPWWKAFDYWGQG TLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTF PAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCD
>9EAJ_3 BAG2 Anti-BRIL Fab Light Chain (chains D) DIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVPS RFSGSRSGTDFTLTISSLQPEDFATYYCQQYLYYSLVTFGQGTKVEIKRTVAAPSVFIFP PSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
Epitope-directed selection of GPCR nanobody ligands with evolvable function. Skiba, M.A., Canavan, C., Nemeth, G.R. et al. Proc Natl Acad Sci U S A (2025) 122:e2423931122-e2423931122. DOI 10.1073/pnas.2423931122 · PubMed
Other PDB entries of the same protein (UniProt P30556 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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