Crystal structure of receptor FcRn bound to Human Astrovirus 6 spike. Determined by X-ray diffraction at 2.97 Å resolution. Released 19 Nov 2025.
Explore 9OC6 in 3D Show helices and sheets RCSB PDB PDBe
9OC6 contains 17 α-helices and 48 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 | 4-11 | 8 | 10 |
| α-helix | 14-15 | 2 | |
| α-helix | 23-25 | 3 | |
| β-strand | 26-27 | 2 | 11 |
| α-helix | 33-35 | 3 | |
| β-strand | 37-42 | 6 | 10 |
| β-strand | 45-48 | 4 | 10 |
| β-strand | 51-61 | 11 | 10 |
| β-strand | 67-68 | 2 | 10 |
| α-helix | 69-74 | 6 | |
| β-strand | 78-81 | 4 | 10 |
| β-strand | 85-98 | 14 | 10 |
| β-strand | 103-114 | 12 | 10 |
| β-strand | 118-125 | 8 | 11 |
| β-strand | 127-128 | 2 | 12 |
| β-strand | 140 | 1 | 13 |
| β-strand | 141-142 | 2 | 12 |
| β-strand | 147-153 | 7 | 11 |
| β-strand | 158-168 | 11 | 10 |
| α-helix | 171-173 | 3 | |
| α-helix | 175-177 | 3 | |
| α-helix | 181-183 | 3 | |
| β-strand | 188 | 1 | 13 |
| α-helix | 200-202 | 3 | |
| β-strand | 206-212 | 7 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-14 | 9 | 1 |
| α-helix | 17-18 | 2 | |
| β-strand | 24-30 | 7 | 1 |
| β-strand | 33-39 | 7 | 1 |
| β-strand | 46-47 | 2 | 1 |
| α-helix | 49-52 | 4 | |
| α-helix | 58-81 | 24 | |
| β-strand | 89-97 | 9 | 1 |
| β-strand | 98 | 1 | 2 |
| β-strand | 104 | 1 | 2 |
| β-strand | 107-112 | 6 | 1 |
| β-strand | 115-121 | 7 | 1 |
| β-strand | 126-128 | 3 | 1 |
| α-helix | 134-142 | 9 | |
| α-helix | 147-153 | 7 | |
| α-helix | 154-158 | 5 | |
| α-helix | 159-166 | 8 | |
| β-strand | 178 | 1 | 3 |
| α-helix | 179-180 | 2 | |
| β-strand | 181-184 | 4 | 4 |
| β-strand | 198-203 | 6 | 4 |
| β-strand | 204 | 1 | 3 |
| β-strand | 208-209 | 2 | 5 |
| β-strand | 225-228 | 4 | 4 |
| β-strand | 234-238 | 5 | 4 |
| β-strand | 252-254 | 3 | 6 |
| β-strand | 255-256 | 2 | 5 |
| β-strand | 263-265 | 3 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 7 |
| α-helix | 4-5 | 2 | |
| β-strand | 6-11 | 6 | 8 |
| β-strand | 21-30 | 10 | 8 |
| β-strand | 31 | 1 | 7 |
| β-strand | 36-41 | 6 | 9 |
| β-strand | 44-45 | 2 | 9 |
| β-strand | 50-51 | 2 | 8 |
| β-strand | 55-56 | 2 | 8 |
| β-strand | 62-70 | 9 | 8 |
| β-strand | 78-83 | 6 | 9 |
| β-strand | 91-94 | 4 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| IgG receptor FcRn large subunit p51 | C | protein | 274 | Homo sapiens | P55899 (AlphaFold model) |
| Beta-2-microglobulin | D | protein | 99 | Homo sapiens | P61769 (AlphaFold model) |
| Capsid polyprotein VP90 | A | protein | 244 | Human astrovirus 6 | A0A3G6VE58 |
>9OC6_1 IgG receptor FcRn large subunit p51 (chains C) AESHLSLLYHLTAVSSPAPGTPAFWVSGWLGPQQYLSYNSLRGEAEPCGAWVWENQVSWY WEKETTDLRIKEKLFLEAFKALGGKGPYTLQGLLGCELGPDNTSVPTAKFALNGEEFMNF DLKQGTWGGDWPEALAISQRWQQQDKAANKELTFLLFSCPHRLREHLERGRGNLEWKEPP SMRLKARPSSPGFSVLTCSAFSFYPPELQLRFLRNGLAAGTGQGDFGPNSDGSFHASSSL TVKSGDEHHYCCIVQHAGLAQPLRVELESPAKSS
>9OC6_2 Beta-2-microglobulin (chains D) IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDW SFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
>9OC6_3 Capsid polyprotein VP90 (chains A) MGETLKVLLTVGNPISPNETNKQTWVNKTIEPPGAVVKIGRDTQHYCTMNGFTLITKVDW FTEEFQPSEEPAPVQGLMVLLDNHKKADVYAAQQYKNPITNDKQQVTSVFLVRVNEGFQV TNHLSYFYRNSVNTDAVENIKIRSATRHTTVRFNQGSWYLLTSTVLHTGPPVSGWLWMNQ ELQNDQAYIIDQGIMHLITPPPVSSQIYFEMATLVPGSGLNDIFEAQKIEWHEGHHHHHH HHHH
Structural hijacking of FcRn by human astrovirus spikes reveals conserved epitopes for broad-spectrum antivirals. Agrawal, S., Jain, M., Marinelli, D. et al. Cell Rep (2025) 44:116679-116679. DOI 10.1016/j.celrep.2025.116679 · PubMed
Other PDB entries of the same protein (UniProt P55899 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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