1NCQ: HRV14 when

The structure of HRV14 when complexed with pleconaril, an antiviral compound. Determined by X-ray diffraction at 2.5 Å resolution. Released 16 Dec 2003.

Method
X-ray diffraction
Resolution
2.5 Å
Organism
Human rhinovirus 14
Chains
4
Atoms
6,537
Mol. weight
94.86 kDa
Ligands
W11
Released
16 Dec 2003

Explore 1NCQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1NCQ contains 39 α-helices and 57 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 A: 14 helices, 17 β-strands

ElementResiduesLengthSheet
β-strand18-2031
β-strand2312
β-strand34-3523
α-helix37-393
α-helix47-493
β-strand5312
β-strand56-5721
α-helix63-653
β-strand6614
α-helix67-704
β-strand75-84105
α-helix93-964
β-strand99-10356
α-helix110-1167
β-strand119-135175
β-strand147-15376
α-helix158-1603
α-helix166-1694
β-strand175-17956
β-strand183-18865
β-strand197-19825
β-strand20317
α-helix215-2173
β-strand223-22866
α-helix231-2322
β-strand237-255195
α-helix257-2582
β-strand25918
α-helix262-2632
α-helix275-2773
α-helix280-2823
Chain B: 13 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand14-1859
β-strand21-2559
β-strand32-33210
α-helix34-363
α-helix41-433
α-helix44-463
α-helix52-532
β-strand54110
α-helix57-593
β-strand64-65210
α-helix66-683
β-strand69-72411
β-strand78-82512
α-helix84-863
α-helix90-989
β-strand99-1111310
β-strand119-1281012
β-strand134113
α-helix144-1474
α-helix150-1523
β-strand154-155212
α-helix159-1602
β-strand165113
α-helix169-1713
β-strand17618
α-helix178-1836
β-strand186-190512
β-strand196-201610
β-strand210110
β-strand21517
β-strand218-2291212
β-strand237-240411
β-strand241-2541410
Chain C: 10 helices, 19 β-strands
ElementResiduesLengthSheet
α-helix6-72
β-strand2315
α-helix30-334
β-strand39-4025
β-strand4214
α-helix43-464
β-strand51-5223
α-helix64-674
β-strand68-7143
β-strand73114
β-strand79-84615
α-helix90-945
α-helix96-1016
β-strand104-108516
β-strand111-11773
β-strand124117
β-strand126-132715
α-helix137-1393
α-helix142-1465
β-strand149-154615
α-helix1551
β-strand160-16563
β-strand174-175216
β-strand186-191615
β-strand195114
β-strand196117
α-helix197-1982
β-strand205-21393
β-strand218-222516
Chain D: 2 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix35-373
α-helix50-534
β-strand56110

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Coat protein VP1Aprotein289Human rhinovirus 14P03303 (AlphaFold model)
Coat protein VP2Bprotein262Human rhinovirus 14P03303 (AlphaFold model)
Coat protein VP3Cprotein236Human rhinovirus 14P03303 (AlphaFold model)
Coat protein VP4Dprotein68Human rhinovirus 14P03303 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1NCQ_1 COAT PROTEIN VP1 (chains A)
GLGDELEEVIVEKTKQTVASISSGPKHTQKVPILTANETGATMPVLPSDSIETRTTYMHF
NGSETDVECFLGRAACVHVTEIQNKDATGIDNHREAKLFNDWKINLSSLVQLRKKLELFT
YVRFDSEYTILATASQPDSANYSSNLVVQAMYVPPGAPNPKEWDDYTWQSASNPSVFFKV
GDTSRFSVPYVGLASAYNCFYDGYSHDDAETQYGITVLNHMGSMAFRIVNEHDEHKTLVK
IRVYHRAKHVEAWIPRAPRALPYTSIGRTNYPKNTEPVIKKRKGDIKSY
Sequence of entity 2 (B), FASTA
>1NCQ_2 COAT PROTEIN VP2 (chains B)
SPNVEACGYSDRVQQITLGNSTITTQEAANAVVCYAEWPEYLPDVDASDVNKTSKPDTSV
CRFYTLDSKTWTTGSKGWCWKLPDALKDMGVFGQNMFFHSLGRSGYTVHVQCNATKFHSG
CLLVVVIPEHQLASHEGGNVSVKYTFTHPGERGIDLSSANEVGGPVKDVLYNMNGTLLGN
LLIFPHQFINLRTNNTATIVIPYINSVPIDSMTRHNNVSLMVIPIAPLTVPTGATPSLPI
TVTIAPMCTEFSGIRSKSIVPQ
Sequence of entity 3 (C), FASTA
>1NCQ_3 COAT PROTEIN VP3 (chains C)
GLPTTTLPGSGQFLTTDDRQSPSALPNYEPTPRIHIPGKVHNLLEIIQVDTLIPMNNTHT
KDEVNSYLIPLNANRQNEQVFGTNLFIGDGVFKTTLLGEIVQYYTHWSGSLRFSLMYTGP
ALSSAKLILAYTPPGARGPQDRREAMLGTHVVWDIGLQSTIVMTIPWTSGVQFRYTDPDT
YTSAGFLSCWYQTSLILPPETTGQVYLLSFISACPDFKLRLMKDTQTISQTVALTE
Sequence of entity 4 (D), FASTA
>1NCQ_4 COAT PROTEIN VP4 (chains D)
GAQVSTQKSGSHENQNILTNGSNQTFTVINYYKDAASTSSAGQSLSMDPSKFTEPVKDLM
LKGAPALN

Ligands and cofactors

IDNameFormulaCopies
W113-{3,5-dimethyl-4-[3-(3-methyl-isoxazol-5-yl)-propoxy]-phenyl}-5-trifluoromethy…C18 H18 F3 N3 O31

Primary citation

Structural and virological studies of the stages of virus replication that are affected by antirhinovirus compounds. Zhang, Y., Simpson, A.A., Ledford, R.M. et al. J Virol (2004) 78:11061-11069. DOI 10.1128/JVI.78.20.11061-11069.2004 · 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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