31LF: HRV virion E2250A mutant

HRV virion E2250A mutant. Determined by electron microscopy at 2.71 Å resolution. Released 9 Sept 2026.

Method
Electron microscopy
Resolution
2.71 Å
Organism
rhinovirus B14
Chains
5
Atoms
6,682
Mol. weight
95.29 kDa
Released
9 Sept 2026

Explore 31LF in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain 1: 10 helices, 22 β-strands

ElementResiduesLengthSheet
β-strand18-2031
β-strand2312
β-strand3113
β-strand34-3524
α-helix37-393
α-helix47-493
β-strand5312
β-strand56-5721
β-strand6615
α-helix67-704
β-strand75-84106
β-strand99-10357
α-helix110-1167
β-strand119-135176
β-strand147-15267
α-helix158-1603
α-helix167-1693
β-strand175-17957
β-strand18018
β-strand18218
β-strand183-18866
β-strand197-19826
β-strand20319
β-strand204110
β-strand213110
β-strand223-22867
β-strand237-255196
α-helix257-2582
β-strand259111
α-helix262-2632
α-helix275-2773
α-helix280-2823
Chain 2: 11 helices, 22 β-strands
ElementResiduesLengthSheet
β-strand14-18512
β-strand21-25512
β-strand31-33313
α-helix34-363
α-helix41-433
α-helix52-532
β-strand54113
α-helix57-593
β-strand64-65213
α-helix66-683
β-strand69-71314
β-strand78-82515
α-helix90-989
β-strand99-1111313
β-strand119116
β-strand121-128815
β-strand134117
α-helix144-1474
β-strand154-155215
α-helix159-1602
β-strand165117
β-strand176111
α-helix178-1836
β-strand186-190515
β-strand196-201613
β-strand210113
β-strand21519
β-strand218-224715
α-helix227-2282
β-strand229116
α-helix230-2312
β-strand238-240314
β-strand241-2541413
Chain 3: 12 helices, 17 β-strands
ElementResiduesLengthSheet
α-helix6-72
β-strand2316
α-helix30-345
β-strand39-4026
β-strand4215
α-helix43-464
β-strand51-5224
α-helix64-674
β-strand68-7144
β-strand79-84618
α-helix90-923
α-helix96-1005
α-helix101-1033
β-strand104-108519
β-strand111-11774
β-strand124-132918
α-helix1331
β-strand134120
β-strand136120
α-helix137-1393
α-helix142-1465
β-strand149-154618
α-helix1551
β-strand160-16564
β-strand174-175219
β-strand186-1961118
α-helix197-1982
β-strand205-21394
β-strand218-222519
Chain 4: 2 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix36-383
α-helix51-544
β-strand57113
β-strand6413

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Capsid protein VP11protein282rhinovirus B14P03303 (AlphaFold model)
Genome polyprotein2protein256rhinovirus B14A0A5B9MV00
Capsid protein VP33protein236rhinovirus B14P03303 (AlphaFold model)
Capsid protein VP44protein47rhinovirus B14P03303 (AlphaFold model)
RNA (5'-r(p*ap*up*up*up*up*up*up*up*up*up*up*up*up*u)-3')5RNA14rhinovirus B14
Sequence of entity 1 (1), FASTA
>31LF_1 Capsid protein VP1 (chains 1)
EVIVEKTKQTVASISSGPKHTQKVPILTANETGATMPVLPSDSIETRTTYMHFNGSETDV
ECFLGRAACVHVTEIQNKDATGIDNHREAKLFNDWKINLSSLVQLRKKLELFTYVRFDSE
YTILATASQPDSANYSSNLVVQAMYVPPGAPNPKEWDDYTWQSASNPSVFFKVGDTSRFS
VPYVGLASAYNCFYDGYSHDDAETQYGITVLNHMGSMAFRIVNEHDEHKTLVKIRVYHRA
KHVEAWIPRAPRALPYTSIGRTNYPKNTEPVIKKRKGDIKSY
Sequence of entity 2 (2), FASTA
>31LF_2 Genome polyprotein (chains 2)
CGYSDRVQQITLGNSTITTQEAANAVVCYAEWPEYLPDVDASDVNKTSKPDTSVCRFYTL
DSKTWTTGSKGWCWKLPDALKDMGVFGQNMFFHSLGRSGYTVHVQCNATKFHSGCLLVVV
IPEHQLASHEGGNVSVKYTFTHPGERGIDLSSANEVGGPVKDVLYNMNGTLLGNLLIFPH
QFINLRTNNTATIVIPYINSVPIDSMTRHNNVSLMVIPIAPLTVPTGATPSLPITVTIAP
MCTAFSGIRSKSIVPQ
Sequence of entity 3 (3), FASTA
>31LF_3 Capsid protein VP3 (chains 3)
GLPTTTLPGSGQFLTTDDRQSPSALPNYEPTPRIHIPGKVHNLLEIIQVDTLIPMNNTHT
KDEVNSYLIPLNANRQNEQVFGTNLFIGDGVFKTTLLGEIVQYYTHWSGSLRFSLMYTGP
ALSSAKLILAYTPPGARGPQDRREAMLGTHVVWDIGLQSTIVMTIPWTSGVQFRYTDPDT
YTSAGFLSCWYQTSLILPPETTGQVYLLSFISACPDFKLRLMKDTQTISQTVALTE
Sequence of entity 4 (4), FASTA
>31LF_4 Capsid protein VP4 (chains 4)
SNQTFTYINYYKDAASTSSAGQSLSMDPSKFTEPVKDLMLKGAPALN
Sequence of entity 5 (5), FASTA
>31LF_5 RNA (5'-R(P*AP*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*U)-3') (chains 5)
AUUUUUUUUUUUUU

Primary citation

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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