Human rhinovirus 2 bound to a concatamer of the VLDL receptor module V3. Determined by X-ray diffraction at 3.5 Å resolution. Released 7 Apr 2009.
Explore 3DPR in 3D Show helices and sheets RCSB PDB PDBe
3DPR contains 28 α-helices and 63 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 |
|---|---|---|---|
| β-strand | 16 | 1 | 1 |
| α-helix | 17-18 | 2 | |
| β-strand | 20 | 1 | 2 |
| α-helix | 41-43 | 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 | 67-71 | 5 | |
| β-strand | 75-83 | 9 | 4 |
| β-strand | 90 | 1 | 5 |
| β-strand | 92 | 1 | 5 |
| β-strand | 94-98 | 5 | 6 |
| α-helix | 106-111 | 6 | |
| β-strand | 114-126 | 13 | 4 |
| β-strand | 129-131 | 3 | 4 |
| β-strand | 140-146 | 7 | 6 |
| β-strand | 148 | 1 | 7 |
| β-strand | 150 | 1 | 7 |
| α-helix | 151-153 | 3 | |
| α-helix | 159-162 | 4 | |
| β-strand | 167-172 | 6 | 6 |
| β-strand | 179-182 | 4 | 4 |
| β-strand | 191-192 | 2 | 4 |
| β-strand | 197 | 1 | 8 |
| α-helix | 207-209 | 3 | |
| β-strand | 215-220 | 6 | 6 |
| β-strand | 229-247 | 19 | 4 |
| α-helix | 249-251 | 3 | |
| β-strand | 257 | 1 | 9 |
| α-helix | 274-276 | 3 | |
| β-strand | 277 | 1 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 15-18 | 4 | 11 |
| β-strand | 21-24 | 4 | 11 |
| β-strand | 32-33 | 2 | 12 |
| α-helix | 34-36 | 3 | |
| β-strand | 54 | 1 | 12 |
| α-helix | 57-59 | 3 | |
| β-strand | 64-65 | 2 | 12 |
| β-strand | 69-72 | 4 | 13 |
| β-strand | 78-80 | 3 | 14 |
| α-helix | 85-87 | 3 | |
| α-helix | 90-98 | 9 | |
| β-strand | 99-111 | 13 | 12 |
| β-strand | 118-126 | 9 | 14 |
| β-strand | 134 | 1 | 15 |
| α-helix | 144-147 | 4 | |
| α-helix | 150-152 | 3 | |
| β-strand | 154-155 | 2 | 14 |
| α-helix | 164-166 | 3 | |
| α-helix | 167 | 1 | |
| β-strand | 168 | 1 | 15 |
| α-helix | 169 | 1 | |
| α-helix | 172-174 | 3 | |
| β-strand | 189-192 | 4 | 14 |
| β-strand | 199-204 | 6 | 12 |
| β-strand | 213-214 | 2 | 12 |
| β-strand | 218 | 1 | 8 |
| β-strand | 223-233 | 11 | 14 |
| β-strand | 239-242 | 4 | 13 |
| β-strand | 243-256 | 14 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 23 | 1 | 4 |
| β-strand | 39-40 | 2 | 4 |
| β-strand | 42 | 1 | 3 |
| α-helix | 43-45 | 3 | |
| β-strand | 51-52 | 2 | 16 |
| α-helix | 53 | 1 | |
| β-strand | 58 | 1 | 10 |
| α-helix | 65-67 | 3 | |
| β-strand | 69-73 | 5 | 16 |
| β-strand | 81-83 | 3 | 17 |
| β-strand | 86 | 1 | 17 |
| α-helix | 94-96 | 3 | |
| α-helix | 98-103 | 6 | |
| β-strand | 106-110 | 5 | 18 |
| β-strand | 113-119 | 7 | 16 |
| β-strand | 126 | 1 | 19 |
| β-strand | 127-134 | 8 | 17 |
| α-helix | 144-148 | 5 | |
| β-strand | 151-157 | 7 | 17 |
| β-strand | 162-167 | 6 | 16 |
| β-strand | 176-177 | 2 | 18 |
| β-strand | 187-192 | 6 | 17 |
| β-strand | 197 | 1 | 19 |
| β-strand | 205-214 | 10 | 16 |
| β-strand | 219-223 | 5 | 18 |
| β-strand | 236 | 1 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-4 | 2 | 20 |
| β-strand | 26-27 | 2 | 20 |
| α-helix | 35-37 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein VP1 | A | protein | 289 | Human rhinovirus 2 | P04936 (AlphaFold model) |
| Protein VP2 | B | protein | 261 | Human rhinovirus 2 | P04936 (AlphaFold model) |
| Protein VP3 | C | protein | 237 | Human rhinovirus 2 | P04936 (AlphaFold model) |
| Protein VP4 | D | protein | 68 | Human rhinovirus 2 | P04936 (AlphaFold model) |
| LDL-receptor class A 3 | E | protein | 39 | Homo sapiens | P98155 (AlphaFold model) |
>3DPR_1 Protein VP1 (chains A) NPVENYIDEVLNEVLVVPNINSSNPTTSNSAPALDAAETGHTSSVQPEDVIETRYVQTSQ TRDEMSLESFLGRSGCIHESKLEVTLANYNKENFTVWAINLQEMAQIRRKFELFTYTRFD SEITLVPCISALSQDIGHITMQYMYVPPGAPVPNSRDDYAWQSGTNASVFWQHGQAYPRF SLPFLSVASAYYMFYDGYDEQDQNYGTANTNNMGSLCSRIVTEKHIHKVHIMTRIYHKAK HVKAWCPRPPRALEYTRAHRTNFKIEDRSIQTAIVTRPIITTAGPSDMY
>3DPR_2 Protein VP2 (chains B) SPTVEACGYSDRIIQITRGDSTITSQDVANAIVAYGVWPHYLSSKDASAIDKPSQPDTSS NRFYTLRSVTWSSSSKGWWWKLPDALKDMGIFGENMFYHYLGRSGYTIHVQCNASKFHQG TLIVALIPEHQIASALHGNVNVGYNYTHPGETGREVKAETRLNPDLQPTEEYWLNFDGTL LGNITIFPHQFINLRSNNSATIIAPYVNAVPMDSMRSHNNWSLVIIPICPLETSSAINTI PITISISPMCAEFSGARAKRQ
>3DPR_3 Protein VP3 (chains C) GLPVFITPGSGQFLTTDDFQSPCALPWYHPTKEISIPGEVKNLVEICQVDSLVPINNTDT YINSENMYSVVLQSSINAPDKIFSIRTDVASQPLATTLIGEISSYFTHWTGSLRFSFMFC GTANTTVKLLLAYTPPGIAEPTTRKDAMLGTHVIWDVGLQSTISMVVPWISASHYRNTSP GRSTSGYITCWYQTRLVIPPQTPPTARLLCFVSGCKDFCLRMARDTNLHLQSGAIAQ
>3DPR_4 Protein VP4 (chains D) GAQVSRQNVGTHSTQNSVSNGSSLNYFNINYFKDAASNGASKLEFTQDPSKFTDPVKDVL EKGIPTLQ
>3DPR_5 LDL-receptor class A 3 (chains E) CRIHEISCGAHSTQCIPVSWRCDGENDCDSGEDEENCGN
Minor group human rhinovirus-receptor interactions: geometry of multimodular attachment and basis of recognition. Querol-Audi, J., Konecsni, T., Pous, J. et al. FEBS Lett (2009) 583:235-240. DOI 10.1016/j.febslet.2008.12.014 · PubMed
Other PDB entries of the same protein (UniProt P04936 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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