Human Rhinovirus 2 bound to a fragment of its cellular receptor protein. Determined by X-ray diffraction at 3.6 Å resolution. Released 4 May 2004.
Explore 1V9U in 3D Show helices and sheets RCSB PDB PDBe
1V9U contains 27 α-helices and 63 β-strands across 5 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 | 16 | 1 | 1 |
| β-strand | 20 | 1 | 2 |
| α-helix | 37-39 | 3 | |
| α-helix | 47-50 | 4 | |
| β-strand | 56 | 1 | 2 |
| β-strand | 61 | 1 | 1 |
| α-helix | 63-65 | 3 | |
| β-strand | 66 | 1 | 3 |
| α-helix | 67-70 | 4 | |
| β-strand | 75-83 | 9 | 4 |
| β-strand | 94-95 | 2 | 5 |
| β-strand | 98 | 1 | 5 |
| α-helix | 106-111 | 6 | |
| β-strand | 114-131 | 18 | 4 |
| β-strand | 140-146 | 7 | 5 |
| β-strand | 148 | 1 | 6 |
| β-strand | 150 | 1 | 6 |
| α-helix | 151-153 | 3 | |
| α-helix | 159-162 | 4 | |
| β-strand | 167-172 | 6 | 5 |
| β-strand | 179-182 | 4 | 4 |
| β-strand | 191-192 | 2 | 4 |
| β-strand | 197 | 1 | 7 |
| α-helix | 207-209 | 3 | |
| β-strand | 215-219 | 5 | 5 |
| β-strand | 229-247 | 19 | 4 |
| α-helix | 249-251 | 3 | |
| β-strand | 257 | 1 | 8 |
| α-helix | 274-276 | 3 | |
| β-strand | 277 | 1 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 15-18 | 4 | 10 |
| β-strand | 21-24 | 4 | 10 |
| β-strand | 32-33 | 2 | 11 |
| α-helix | 34-36 | 3 | |
| β-strand | 54 | 1 | 11 |
| α-helix | 57-59 | 3 | |
| β-strand | 64-65 | 2 | 11 |
| β-strand | 69-72 | 4 | 12 |
| β-strand | 78-80 | 3 | 13 |
| α-helix | 90-98 | 9 | |
| β-strand | 99-111 | 13 | 11 |
| β-strand | 121-126 | 6 | 13 |
| β-strand | 134 | 1 | 14 |
| α-helix | 144-147 | 4 | |
| β-strand | 154-155 | 2 | 13 |
| α-helix | 167 | 1 | |
| β-strand | 168 | 1 | 14 |
| α-helix | 169 | 1 | |
| α-helix | 172-174 | 3 | |
| α-helix | 184-186 | 3 | |
| β-strand | 189-192 | 4 | 13 |
| β-strand | 199-204 | 6 | 11 |
| β-strand | 213-214 | 2 | 11 |
| β-strand | 218 | 1 | 7 |
| β-strand | 223-229 | 7 | 13 |
| β-strand | 239-242 | 4 | 12 |
| β-strand | 243-256 | 14 | 11 |
| α-helix | 258-260 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 23 | 1 | 4 |
| α-helix | 31-33 | 3 | |
| β-strand | 39-40 | 2 | 4 |
| β-strand | 42 | 1 | 3 |
| α-helix | 44-47 | 4 | |
| β-strand | 51-52 | 2 | 15 |
| β-strand | 58 | 1 | 9 |
| α-helix | 65-67 | 3 | |
| β-strand | 69-73 | 5 | 15 |
| β-strand | 81-83 | 3 | 16 |
| β-strand | 86 | 1 | 16 |
| α-helix | 94-96 | 3 | |
| α-helix | 98-103 | 6 | |
| β-strand | 106-110 | 5 | 17 |
| β-strand | 113-119 | 7 | 15 |
| β-strand | 126 | 1 | 18 |
| β-strand | 128 | 1 | 19 |
| β-strand | 129-134 | 6 | 16 |
| α-helix | 144-148 | 5 | |
| β-strand | 151-153 | 3 | 16 |
| β-strand | 156 | 1 | 19 |
| β-strand | 164-167 | 4 | 15 |
| β-strand | 176-177 | 2 | 17 |
| β-strand | 187-192 | 6 | 16 |
| β-strand | 197 | 1 | 18 |
| β-strand | 205-214 | 10 | 15 |
| β-strand | 219-223 | 5 | 17 |
| β-strand | 236 | 1 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-4 | 2 | 20 |
| β-strand | 26-27 | 2 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 130-132 | 3 | |
| α-helix | 144-146 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Coat protein VP1 | 1 | protein | 289 | Human rhinovirus 2 | P04936 (AlphaFold model) |
| Coat protein VP2 | 2 | protein | 261 | Human rhinovirus 2 | P04936 (AlphaFold model) |
| Coat protein VP3 | 3 | protein | 237 | Human rhinovirus 2 | P04936 (AlphaFold model) |
| Coat protein VP4 | 4 | protein | 68 | Human rhinovirus 2 | P04936 (AlphaFold model) |
| LDL-receptor class A 3 | 5 | protein | 41 | Homo sapiens | P98155 (AlphaFold model) |
>1V9U_1 Coat protein VP1 (chains 1) NPVENYIDEVLNEVLVVPNINSSNPTTSNSAPALDAAETGHTSSVQPEDVIETRYVQTSQ TRDEMSLESFLGRSGCIHESKLEVTLANYNKENFTVWAINLQEMAQIRRKFELFTYTRFD SEITLVPCISALSQDIGHITMQYMYVPPGAPVPNSRDDYAWQSGTNASVFWQHGQAYPRF SLPFLSVASAYYMFYDGYDEQDQNYGTANTNNMGSLCSRIVTEKHIHKVHIMTRIYHKAK HVKAWCPRPPRALEYTRAHRTNFKIEDRSIQTAIVTRPIITTAGPSDMY
>1V9U_2 Coat protein VP2 (chains 2) SPTVEACGYSDRIIQITRGDSTITSQDVANAIVAYGVWPHYLSSKDASAIDKPSQPDTSS NRFYTLRSVTWSSSSKGWWWKLPDALKDMGIFGENMFYHYLGRSGYTIHVQCNASKFHQG TLIVALIPEHQIASALHGNVNVGYNYTHPGETGREVKAETRLNPDLQPTEEYWLNFDGTL LGNITIFPHQFINLRSNNSATIIAPYVNAVPMDSMRSHNNWSLVIIPICPLETSSAINTI PITISISPMCAEFSGARAKRQ
>1V9U_3 Coat protein VP3 (chains 3) GLPVFITPGSGQFLTTDDFQSPCALPWYHPTKEISIPGEVKNLVEICQVDSLVPINNTDT YINSENMYSVVLQSSINAPDKIFSIRTDVASQPLATTLIGEISSYFTHWTGSLRFSFMFC GTANTTVKLLLAYTPPGIAEPTTRKDAMLGTHVIWDVGLQSTISMVVPWISASHYRNTSP GRSTSGYITCWYQTRLVIPPQTPPTARLLCFVSGCKDFCLRMARDTNLHLQSGAIAQ
>1V9U_4 Coat protein VP4 (chains 4) GAQVSRQNVGTHSTQNSVSNGSSLNYFNINYFKDAASNGASKLEFTQDPSKFTDPVKDVL EKGIPTLQ
>1V9U_5 LDL-receptor class A 3 (chains 5) RTCRIHEISCGAHSTQCIPVSWRCDGENDCDSGEDEENCGN
X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein. Verdaguer, N., Fita, I., Reithmayer, M. et al. Nat Struct Mol Biol (2004) 11:429-434. DOI 10.1038/nsmb753 · PubMed
Other PDB entries of the same protein (UniProt P04936 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1V9U directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.