Integrated illustration of a valid epitope based on the SLA class I structure and tetramer technique could carry forward the development of molecular vaccine in swine species. Determined by X-ray diffraction at 2.2 Å resolution. Released 24 Oct 2018.
Explore 5YLX in 3D Show helices and sheets RCSB PDB PDBe
5YLX contains 14 α-helices and 30 β-strands across 2 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 | 4-14 | 11 | 1 |
| α-helix | 15-17 | 3 | |
| β-strand | 19-28 | 10 | 1 |
| β-strand | 31-37 | 7 | 1 |
| β-strand | 46-47 | 2 | 1 |
| α-helix | 50-54 | 5 | |
| α-helix | 57-85 | 29 | |
| β-strand | 94-103 | 10 | 1 |
| β-strand | 109-118 | 10 | 1 |
| β-strand | 121-126 | 6 | 1 |
| β-strand | 133-135 | 3 | 1 |
| α-helix | 138-149 | 12 | |
| α-helix | 152-159 | 8 | |
| α-helix | 160-164 | 5 | |
| α-helix | 165-174 | 10 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 2 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-193 | 8 | 3 |
| β-strand | 199-208 | 10 | 3 |
| β-strand | 209 | 1 | 2 |
| β-strand | 214-219 | 6 | 4 |
| β-strand | 223 | 1 | 4 |
| β-strand | 229-230 | 2 | 3 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 3 |
| β-strand | 241-248 | 8 | 3 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 4 |
| β-strand | 270-272 | 3 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 5 |
| α-helix | 4-5 | 2 | |
| β-strand | 6-11 | 6 | 6 |
| β-strand | 21-30 | 10 | 6 |
| β-strand | 31 | 1 | 5 |
| β-strand | 36-41 | 6 | 7 |
| β-strand | 44-45 | 2 | 7 |
| α-helix | 46-47 | 2 | |
| β-strand | 49-50 | 2 | 6 |
| α-helix | 51-53 | 3 | |
| β-strand | 54-55 | 2 | 6 |
| β-strand | 61-69 | 9 | 6 |
| β-strand | 77-82 | 6 | 7 |
| β-strand | 90-93 | 4 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| MHC class I antigen | A | protein | 275 | Sus scrofa | H6TIB1 (AlphaFold model) |
| Beta-2-microglobulin | B | protein | 98 | Sus scrofa | Q07717 (AlphaFold model) |
| PRRSV-NSP9-TMP9 peptide | C | protein | 9 | Porcine reproductive and respiratory syndrome virus | Q9YN02 |
>5YLX_1 MHC class I antigen (chains A) GPHSLSYFSTAVSRPDRGDSRFIAVGYVDDTQFVRFDSDAPNPRMEPRVPWIQQEGQEYW AEETRKVKDNAQTYRVNLKALRGYYNQSVAGSHTLQSMFGCYLGPDGLLLHGYRQDAYDG ADYIALNEDLRSWTAADMAAQITKRKWEAADAAEQMRSYLQGLCVESLRKYLEMGKDTLQ RAEPPKTHVTRHPSSDLGATLRCWALGFYPKEISLTWQREGQDQSQDMELVETRPSGDGT FQKWAALVVPPGEEQSYTCHVQHEGLQEPLTLRWD
>5YLX_2 Beta-2-microglobulin (chains B) VARPPKVQVYSRHPAENGKPNYLNCYVSGFHPPQIEIDLLKNGEKMNAEQSDLSFSKDWS FYLLVHTEFTPNAVDQYSCRVKHVTLDKPKIVKWDRDH
>5YLX_3 PRRSV-NSP9-TMP9 peptide (chains C) TMPPGFELY
Illumination of PRRSV Cytotoxic T Lymphocyte Epitopes by the Three-Dimensional Structure and Peptidome of Swine Lymphocyte Antigen Class I (SLA-I). Pan, X., Zhang, N., Wei, X. et al. Front Immunol (2019) 10:2995-2995. DOI 10.3389/fimmu.2019.02995 · PubMed
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