HRV14 3C in complex with single chain antibody YDF. Determined by X-ray diffraction at 1.84 Å resolution. Released 27 May 2020.
Explore 6KYZ in 3D Show helices and sheets RCSB PDB PDBe
6KYZ contains 26 α-helices and 80 β-strands across 6 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 | 5-13 | 9 | |
| β-strand | 15-20 | 6 | 1 |
| β-strand | 23-31 | 9 | 1 |
| β-strand | 32 | 1 | 2 |
| β-strand | 34-38 | 5 | 1 |
| α-helix | 39-41 | 3 | |
| β-strand | 46-49 | 4 | 1 |
| β-strand | 52-63 | 12 | 1 |
| β-strand | 69-77 | 9 | 1 |
| α-helix | 81-82 | 2 | |
| β-strand | 83 | 1 | 2 |
| α-helix | 84 | 1 | |
| α-helix | 87-89 | 3 | |
| β-strand | 90 | 1 | 1 |
| β-strand | 95 | 1 | 3 |
| β-strand | 98-105 | 8 | 1 |
| β-strand | 108-117 | 10 | 1 |
| β-strand | 118 | 1 | 3 |
| β-strand | 119-126 | 8 | 1 |
| β-strand | 129-138 | 10 | 1 |
| α-helix | 143-145 | 3 | |
| α-helix | 148 | 1 | |
| β-strand | 149-152 | 4 | 1 |
| β-strand | 155-163 | 9 | 1 |
| β-strand | 167-172 | 6 | 1 |
| α-helix | 173 | 1 | |
| α-helix | 175-177 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-9 | 5 | 4 |
| β-strand | 12-14 | 3 | 1 |
| β-strand | 20-27 | 8 | 4 |
| α-helix | 31-33 | 3 | |
| β-strand | 36-41 | 6 | 1 |
| β-strand | 47-53 | 7 | 1 |
| β-strand | 60-62 | 3 | 1 |
| β-strand | 71-75 | 5 | 4 |
| β-strand | 80-85 | 6 | 4 |
| α-helix | 90-92 | 3 | |
| β-strand | 94-107 | 14 | 1 |
| β-strand | 113-118 | 6 | 1 |
| β-strand | 122-126 | 5 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5 | 1 | 5 |
| β-strand | 9-12 | 4 | 6 |
| β-strand | 17-23 | 7 | 5 |
| α-helix | 27-29 | 3 | |
| β-strand | 31-37 | 7 | 6 |
| β-strand | 44-47 | 4 | 6 |
| β-strand | 48 | 1 | 7 |
| β-strand | 52 | 1 | 7 |
| β-strand | 61-66 | 6 | 5 |
| β-strand | 69-75 | 7 | 5 |
| α-helix | 79-81 | 3 | |
| β-strand | 83-91 | 9 | 6 |
| β-strand | 94-97 | 4 | 6 |
| β-strand | 101-105 | 5 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-13 | 7 | |
| β-strand | 15-20 | 6 | 8 |
| β-strand | 23-31 | 9 | 8 |
| β-strand | 32 | 1 | 9 |
| β-strand | 34-38 | 5 | 8 |
| α-helix | 39-41 | 3 | |
| β-strand | 46-49 | 4 | 8 |
| β-strand | 52-63 | 12 | 8 |
| β-strand | 69-78 | 10 | 8 |
| α-helix | 82 | 1 | |
| β-strand | 83 | 1 | 9 |
| α-helix | 84 | 1 | |
| α-helix | 87-89 | 3 | |
| β-strand | 90 | 1 | 8 |
| β-strand | 95 | 1 | 8 |
| β-strand | 98-105 | 8 | 8 |
| β-strand | 108-126 | 19 | 8 |
| β-strand | 129-138 | 10 | 8 |
| α-helix | 143-145 | 3 | |
| α-helix | 148 | 1 | |
| β-strand | 149-152 | 4 | 8 |
| β-strand | 155-163 | 9 | 8 |
| β-strand | 167-172 | 6 | 8 |
| α-helix | 173 | 1 | |
| α-helix | 175-177 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-9 | 5 | 10 |
| β-strand | 12-14 | 3 | 8 |
| β-strand | 20-27 | 8 | 10 |
| α-helix | 31-33 | 3 | |
| β-strand | 36-41 | 6 | 8 |
| β-strand | 47-53 | 7 | 8 |
| β-strand | 60-62 | 3 | 8 |
| β-strand | 70-75 | 6 | 10 |
| β-strand | 80-85 | 6 | 10 |
| α-helix | 90-92 | 3 | |
| β-strand | 94-107 | 14 | 8 |
| β-strand | 113-118 | 6 | 8 |
| β-strand | 122-126 | 5 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Genome polyprotein | A, D | protein | 184 | Human rhinovirus 14 | P03303 (AlphaFold model) |
| YDF H chain | B, E | protein | 145 | Homo sapiens | |
| YDF L chain | C, F | protein | 107 | Homo sapiens |
>6KYZ_1 Genome polyprotein (chains A, D) GSGPNTEFALSLLRKNIMTITTSKGEFTGLGIHDRVCVIPTHAQPGDDVLVNGQKIRVKD KYKLVDPENINLELTVLTLDRNEKFRDIRGFISEDLEGVDATLVVHSNNFTNTILEVGPV TMAGLINLSSTPTNRMIRYDYATKTGQCGGVLCATGKIFGIHVGGNGRQGFSAQLKKQYF VEKQ
>6KYZ_2 YDF H chain (chains B, E) SNMAQVQLLQSGGGVVQPGRSLRLSCAASGFTFSSYAMHWVRQAPGKGLEWVAVISYDGS NKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARVGKGGYDFWSGSGYMDVW GKGTTVTVSSGGGGSGGGGSGGGGS
>6KYZ_3 YDF L chain (chains C, F) SYVLTQPPSVSVSPGQTASITCSGDKLGDKYACWYQQKPGQSPVLVIYQDSKRPSGIPER FSGSNSGNTATLTISGTQAMDEADYYCQAWDSSTVVFGGGTKLTVLG
Inhibitory antibodies identify unique sites of therapeutic vulnerability in rhinovirus and other enteroviruses. Meng, B., Lan, K., Xie, J. et al. Proc Natl Acad Sci U S A (2020) 117:13499-13508. DOI 10.1073/pnas.1918844117 · 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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