HRV virion E2250A mutant. Determined by electron microscopy at 2.71 Å resolution. Released 9 Sept 2026.
Explore 31LF in 3D Show helices and sheets RCSB PDB PDBe
31LF contains 35 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 | 18-20 | 3 | 1 |
| β-strand | 23 | 1 | 2 |
| β-strand | 31 | 1 | 3 |
| β-strand | 34-35 | 2 | 4 |
| α-helix | 37-39 | 3 | |
| α-helix | 47-49 | 3 | |
| β-strand | 53 | 1 | 2 |
| β-strand | 56-57 | 2 | 1 |
| β-strand | 66 | 1 | 5 |
| α-helix | 67-70 | 4 | |
| β-strand | 75-84 | 10 | 6 |
| β-strand | 99-103 | 5 | 7 |
| α-helix | 110-116 | 7 | |
| β-strand | 119-135 | 17 | 6 |
| β-strand | 147-152 | 6 | 7 |
| α-helix | 158-160 | 3 | |
| α-helix | 167-169 | 3 | |
| β-strand | 175-179 | 5 | 7 |
| β-strand | 180 | 1 | 8 |
| β-strand | 182 | 1 | 8 |
| β-strand | 183-188 | 6 | 6 |
| β-strand | 197-198 | 2 | 6 |
| β-strand | 203 | 1 | 9 |
| β-strand | 204 | 1 | 10 |
| β-strand | 213 | 1 | 10 |
| β-strand | 223-228 | 6 | 7 |
| β-strand | 237-255 | 19 | 6 |
| α-helix | 257-258 | 2 | |
| β-strand | 259 | 1 | 11 |
| α-helix | 262-263 | 2 | |
| α-helix | 275-277 | 3 | |
| α-helix | 280-282 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 14-18 | 5 | 12 |
| β-strand | 21-25 | 5 | 12 |
| β-strand | 31-33 | 3 | 13 |
| α-helix | 34-36 | 3 | |
| α-helix | 41-43 | 3 | |
| α-helix | 52-53 | 2 | |
| β-strand | 54 | 1 | 13 |
| α-helix | 57-59 | 3 | |
| β-strand | 64-65 | 2 | 13 |
| α-helix | 66-68 | 3 | |
| β-strand | 69-71 | 3 | 14 |
| β-strand | 78-82 | 5 | 15 |
| α-helix | 90-98 | 9 | |
| β-strand | 99-111 | 13 | 13 |
| β-strand | 119 | 1 | 16 |
| β-strand | 121-128 | 8 | 15 |
| β-strand | 134 | 1 | 17 |
| α-helix | 144-147 | 4 | |
| β-strand | 154-155 | 2 | 15 |
| α-helix | 159-160 | 2 | |
| β-strand | 165 | 1 | 17 |
| β-strand | 176 | 1 | 11 |
| α-helix | 178-183 | 6 | |
| β-strand | 186-190 | 5 | 15 |
| β-strand | 196-201 | 6 | 13 |
| β-strand | 210 | 1 | 13 |
| β-strand | 215 | 1 | 9 |
| β-strand | 218-224 | 7 | 15 |
| α-helix | 227-228 | 2 | |
| β-strand | 229 | 1 | 16 |
| α-helix | 230-231 | 2 | |
| β-strand | 238-240 | 3 | 14 |
| β-strand | 241-254 | 14 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-7 | 2 | |
| β-strand | 23 | 1 | 6 |
| α-helix | 30-34 | 5 | |
| β-strand | 39-40 | 2 | 6 |
| β-strand | 42 | 1 | 5 |
| α-helix | 43-46 | 4 | |
| β-strand | 51-52 | 2 | 4 |
| α-helix | 64-67 | 4 | |
| β-strand | 68-71 | 4 | 4 |
| β-strand | 79-84 | 6 | 18 |
| α-helix | 90-92 | 3 | |
| α-helix | 96-100 | 5 | |
| α-helix | 101-103 | 3 | |
| β-strand | 104-108 | 5 | 19 |
| β-strand | 111-117 | 7 | 4 |
| β-strand | 124-132 | 9 | 18 |
| α-helix | 133 | 1 | |
| β-strand | 134 | 1 | 20 |
| β-strand | 136 | 1 | 20 |
| α-helix | 137-139 | 3 | |
| α-helix | 142-146 | 5 | |
| β-strand | 149-154 | 6 | 18 |
| α-helix | 155 | 1 | |
| β-strand | 160-165 | 6 | 4 |
| β-strand | 174-175 | 2 | 19 |
| β-strand | 186-196 | 11 | 18 |
| α-helix | 197-198 | 2 | |
| β-strand | 205-213 | 9 | 4 |
| β-strand | 218-222 | 5 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 36-38 | 3 | |
| α-helix | 51-54 | 4 | |
| β-strand | 57 | 1 | 13 |
| β-strand | 64 | 1 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Capsid protein VP1 | 1 | protein | 282 | rhinovirus B14 | P03303 (AlphaFold model) |
| Genome polyprotein | 2 | protein | 256 | rhinovirus B14 | A0A5B9MV00 |
| Capsid protein VP3 | 3 | protein | 236 | rhinovirus B14 | P03303 (AlphaFold model) |
| Capsid protein VP4 | 4 | protein | 47 | rhinovirus B14 | P03303 (AlphaFold model) |
| RNA (5'-r(p*ap*up*up*up*up*up*up*up*up*up*up*up*up*u)-3') | 5 | RNA | 14 | rhinovirus B14 |
>31LF_1 Capsid protein VP1 (chains 1) EVIVEKTKQTVASISSGPKHTQKVPILTANETGATMPVLPSDSIETRTTYMHFNGSETDV ECFLGRAACVHVTEIQNKDATGIDNHREAKLFNDWKINLSSLVQLRKKLELFTYVRFDSE YTILATASQPDSANYSSNLVVQAMYVPPGAPNPKEWDDYTWQSASNPSVFFKVGDTSRFS VPYVGLASAYNCFYDGYSHDDAETQYGITVLNHMGSMAFRIVNEHDEHKTLVKIRVYHRA KHVEAWIPRAPRALPYTSIGRTNYPKNTEPVIKKRKGDIKSY
>31LF_2 Genome polyprotein (chains 2) CGYSDRVQQITLGNSTITTQEAANAVVCYAEWPEYLPDVDASDVNKTSKPDTSVCRFYTL DSKTWTTGSKGWCWKLPDALKDMGVFGQNMFFHSLGRSGYTVHVQCNATKFHSGCLLVVV IPEHQLASHEGGNVSVKYTFTHPGERGIDLSSANEVGGPVKDVLYNMNGTLLGNLLIFPH QFINLRTNNTATIVIPYINSVPIDSMTRHNNVSLMVIPIAPLTVPTGATPSLPITVTIAP MCTAFSGIRSKSIVPQ
>31LF_3 Capsid protein VP3 (chains 3) GLPTTTLPGSGQFLTTDDRQSPSALPNYEPTPRIHIPGKVHNLLEIIQVDTLIPMNNTHT KDEVNSYLIPLNANRQNEQVFGTNLFIGDGVFKTTLLGEIVQYYTHWSGSLRFSLMYTGP ALSSAKLILAYTPPGARGPQDRREAMLGTHVVWDIGLQSTIVMTIPWTSGVQFRYTDPDT YTSAGFLSCWYQTSLILPPETTGQVYLLSFISACPDFKLRLMKDTQTISQTVALTE
>31LF_4 Capsid protein VP4 (chains 4) SNQTFTYINYYKDAASTSSAGQSLSMDPSKFTEPVKDLMLKGAPALN
>31LF_5 RNA (5'-R(P*AP*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*U)-3') (chains 5) AUUUUUUUUUUUUU
RNA-repelling Anionic Clusters in Human Rhinovirus Cooperate with Cationic Residues to Promote Virion Assembly and Restrain RNA Release. Riomoros-Barahona, V., Martinez-Romero, J.M., Valiente, L. et al. J Mol Biol (2026) 438:169998-169998. DOI 10.1016/j.jmb.2026.169998 · PubMed
Other PDB entries of the same protein (UniProt P03303 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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