Human rhinovirus 16 coat protein in complex with antiviral compound VP61209. Determined by X-ray diffraction at 2.8 Å resolution. Released 20 Jul 1999.
Explore 1QJU in 3D Show helices and sheets RCSB PDB PDBe
1QJU contains 37 α-helices and 62 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 | 2-11 | 10 | |
| β-strand | 16 | 1 | 1 |
| α-helix | 17-19 | 3 | |
| β-strand | 20 | 1 | 2 |
| β-strand | 34-35 | 2 | 3 |
| 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 | 4 |
| α-helix | 67-71 | 5 | |
| β-strand | 75-83 | 9 | 5 |
| α-helix | 88-91 | 4 | |
| β-strand | 93-97 | 5 | 6 |
| α-helix | 104-110 | 7 | |
| β-strand | 113-130 | 18 | 5 |
| β-strand | 139-145 | 7 | 6 |
| α-helix | 150-152 | 3 | |
| α-helix | 158-161 | 4 | |
| β-strand | 167-171 | 5 | 6 |
| α-helix | 175-177 | 3 | |
| β-strand | 178-181 | 4 | 5 |
| β-strand | 190-191 | 2 | 5 |
| β-strand | 196 | 1 | 7 |
| β-strand | 197 | 1 | 8 |
| β-strand | 206 | 1 | 8 |
| β-strand | 216-221 | 6 | 6 |
| α-helix | 224-225 | 2 | |
| β-strand | 230-248 | 19 | 5 |
| α-helix | 250-251 | 2 | |
| β-strand | 252 | 1 | 9 |
| β-strand | 258 | 1 | 10 |
| β-strand | 264 | 1 | 11 |
| α-helix | 270-272 | 3 | |
| α-helix | 276-278 | 3 | |
| β-strand | 279 | 1 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 14-18 | 5 | 13 |
| β-strand | 21-25 | 5 | 13 |
| β-strand | 32-33 | 2 | 14 |
| α-helix | 34-36 | 3 | |
| α-helix | 41-43 | 3 | |
| α-helix | 52-53 | 2 | |
| β-strand | 54 | 1 | 14 |
| α-helix | 57-59 | 3 | |
| β-strand | 64-65 | 2 | 14 |
| β-strand | 69-71 | 3 | 15 |
| β-strand | 78-82 | 5 | 16 |
| α-helix | 84-86 | 3 | |
| α-helix | 90-98 | 9 | |
| β-strand | 99-111 | 13 | 14 |
| β-strand | 119-128 | 10 | 16 |
| β-strand | 135 | 1 | 11 |
| α-helix | 140-143 | 4 | |
| α-helix | 144-147 | 4 | |
| α-helix | 150-152 | 3 | |
| β-strand | 154-155 | 2 | 16 |
| α-helix | 165-167 | 3 | |
| α-helix | 170-172 | 3 | |
| β-strand | 177 | 1 | 9 |
| α-helix | 179-184 | 6 | |
| β-strand | 187-191 | 5 | 16 |
| β-strand | 197-202 | 6 | 14 |
| β-strand | 211 | 1 | 14 |
| β-strand | 216 | 1 | 7 |
| β-strand | 219-230 | 12 | 16 |
| β-strand | 238-240 | 3 | 15 |
| β-strand | 241-254 | 14 | 14 |
| α-helix | 257-258 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-7 | 2 | |
| β-strand | 23 | 1 | 5 |
| α-helix | 30-33 | 4 | |
| β-strand | 39-40 | 2 | 5 |
| β-strand | 42 | 1 | 4 |
| α-helix | 44-47 | 4 | |
| β-strand | 51-52 | 2 | 3 |
| β-strand | 58 | 1 | 12 |
| α-helix | 65-68 | 4 | |
| β-strand | 69-72 | 4 | 3 |
| β-strand | 81-86 | 6 | 17 |
| α-helix | 98-103 | 6 | |
| β-strand | 106-110 | 5 | 18 |
| β-strand | 113-119 | 7 | 3 |
| β-strand | 126 | 1 | 19 |
| β-strand | 128-134 | 7 | 17 |
| α-helix | 139-141 | 3 | |
| α-helix | 144-148 | 5 | |
| β-strand | 151-156 | 6 | 17 |
| β-strand | 162-167 | 6 | 3 |
| β-strand | 176-177 | 2 | 18 |
| β-strand | 188-193 | 6 | 17 |
| β-strand | 198 | 1 | 19 |
| β-strand | 207-215 | 9 | 3 |
| β-strand | 220-224 | 5 | 18 |
| β-strand | 237 | 1 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-5 | 4 | 20 |
| β-strand | 26-29 | 4 | 20 |
| α-helix | 35-37 | 3 | |
| α-helix | 41-43 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein VP1 | 1 | protein | 285 | HUMAN RHINOVIRUS 16 | Q82122 (AlphaFold model) |
| Protein VP2 | 2 | protein | 261 | HUMAN RHINOVIRUS 16 | Q82122 (AlphaFold model) |
| Protein VP3 | 3 | protein | 238 | HUMAN RHINOVIRUS 16 | Q82122 (AlphaFold model) |
| Protein VP4 | 4 | protein | 68 | HUMAN RHINOVIRUS 16 | Q82122 (AlphaFold model) |
>1QJU_1 PROTEIN VP1 (chains 1) NPVERYVDEVLNEVLVVPNINQSHPTTSNAAPVLDAAETGHTNKIQPEDTIETRYVQSSQ TLDEMSVESFLGRSGCIHESVLDIVDNYNDQSFTKWNINLQEMAQIRRKFEMFTYARFDS EITMVPSVAAKDGHIGHIVMQYMYVPPGAPIPTTRDDYAWQSGTNASVFWQHGQPFPRFS LPFLSIASAYYMFYDGYDGDTYKSRYGTVVTNDMGTLCSRIVTSEQLHKVKVVTRIYHKA KHTKAWCPRPPRAVQYSHTHTTNYKLSSEVHNDVAIRPRTNLTTV
>1QJU_2 PROTEIN VP2 (chains 2) SPSVEACGYSDRIIQITRGDSTITSQDVANAVVGYGVWPHYLTPQDATAIDKPTQPDTSS NRFYTLDSKMWNSTSKGWWWKLPDALKDMGIFGENMFYHFLGRSGYTVHVQCNASKFHQG TLLVVMIPEHQLATVNKGNVNAGYKYTHPGEAGREVGTQVENEKQPSDDNWLNFDGTLLG NLLIFPHQFINLRSNNSATLIVPYVNAVPMDSMVRHNNWSLVIIPVCQLQSNNISNIVPI TVSISPMCAEFSGARAKTVVQ
>1QJU_3 PROTEIN VP3 (chains 3) GLPVYVTPGSGQFMTTDDMQSPCALPWYHPTKEIFIPGEVKNLIEMCQVDTLIPINSTQS NIGNVSMYTVTLSPQTKLAEEIFAIKVDIASHPLATTLIGEIASYFTHWTGSLRFSFMFC GTANTTLKVLLAYTPPGIGKPRSRKEAMLGTHVVWDVGLQSTVSLVVPWISASQYRFTTP DTYSSAGYITCWYQTNFVVPPNTPNTAEMLCFVSGCKDFCLRMARDTDLHKQTGPITQ
>1QJU_4 PROTEIN VP4 (chains 4) GAQVSRQNVGTHSTQNMVSNGSSLNYFNINYFKDAASSGASRLDFSQDPSKFTDPVKDVL EKGIPTLQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 1 |
| W01 | 2,6-dimethyl-1-(3-[3-methyl-5-isoxazolyl]-propanyl)-4-[2N-methyl-2H-tetrazol-5-… | C17 H21 N5 O2 | 1 |
| MYR | Myristic acid | C14 H28 O2 | 1 |
Analysis of Three Structurally Related Antiviral Compounds in Complex with Human Rhinovirus 16. Hadfield, A.T., Minor, I., Diana, G.D. et al. Proc Natl Acad Sci U S A (1999) 96:14730. DOI 10.1073/PNAS.96.26.14730 · PubMed
Other PDB entries of the same protein (UniProt Q82122 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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