Crystal structure of the Middle East respiratory syndrome coronavirus papain-like protease bound to ubiquitin variant ME.4. Determined by X-ray diffraction at 2.55 Å resolution. Released 10 May 2017.
Explore 5V69 in 3D Show helices and sheets RCSB PDB PDBe
5V69 contains 17 α-helices and 28 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 | 1484-1490 | 7 | 1 |
| β-strand | 1497-1502 | 6 | 1 |
| α-helix | 1507-1510 | 4 | |
| β-strand | 1514-1516 | 3 | 1 |
| β-strand | 1519-1520 | 2 | 1 |
| α-helix | 1525-1526 | 2 | |
| α-helix | 1528-1530 | 3 | |
| β-strand | 1534-1537 | 4 | 1 |
| α-helix | 1543-1553 | 11 | |
| α-helix | 1560-1570 | 11 | |
| α-helix | 1571-1573 | 3 | |
| β-strand | 1576-1579 | 4 | 2 |
| β-strand | 1582-1585 | 4 | 2 |
| α-helix | 1586-1587 | 2 | |
| α-helix | 1592-1601 | 10 | |
| β-strand | 1607-1609 | 3 | 3 |
| α-helix | 1612-1622 | 11 | |
| α-helix | 1627-1636 | 10 | |
| α-helix | 1647-1655 | 9 | |
| β-strand | 1658-1660 | 3 | 3 |
| β-strand | 1665-1672 | 8 | 4 |
| β-strand | 1676-1683 | 8 | 4 |
| α-helix | 1684-1688 | 5 | |
| β-strand | 1689-1691 | 3 | 5 |
| α-helix | 1696-1699 | 4 | |
| β-strand | 1703-1706 | 4 | 4 |
| β-strand | 1712-1721 | 10 | 4 |
| β-strand | 1724-1737 | 14 | 5 |
| β-strand | 1746-1751 | 6 | 5 |
| β-strand | 1759-1766 | 8 | 5 |
| β-strand | 1769-1773 | 5 | 5 |
| β-strand | 1778-1781 | 4 | 5 |
| β-strand | 1783-1794 | 12 | 5 |
| β-strand | 1797-1799 | 3 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 6 |
| β-strand | 12-16 | 5 | 6 |
| β-strand | 22 | 1 | 7 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 6 |
| β-strand | 48-49 | 2 | 6 |
| α-helix | 50-51 | 2 | |
| β-strand | 55 | 1 | 7 |
| β-strand | 66-71 | 6 | 6 |
| α-helix | 72 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| MERS-CoV PLpro | A | protein | 324 | Human betacoronavirus 2c EMC/2012 | K0BWD0 (AlphaFold model) |
| ME.4 | B | protein | 104 | Homo sapiens |
>5V69_1 MERS-CoV PLpro (chains A) TQQLTIEVLVTVDGVNFRTVVLNNKNTYRSQLGCVFFNGADISDTIPDEKQNGHSLYLAD NLTADETKALKELYGPVDPTFLHRFYSLKAAVHGWKMVVCDKVRSLKLSDNNCYLNAVIM TLDLLKDIKFVIPALQHAFMKHKGGDSTDFIALIMAYGNCTFGAPDDASRLLHTVLAKAE LCCSARMVWREWCNVCGIKDVVLQGLKACCYVGVQTVEDLRARMTYVCQCGGERHRQLVE HTTPWLLLSGTPNEKLVTTSTAPDFVAFNVFQGIETAVGHYVHARLKGGLILKFDSGTVS KTSDWKCKVTDVLFPGQKYSSDCN
>5V69_2 ME.4 (chains B) MAHHHHHHVTSLYKKAGSTDYKDDDDKMRIFVETLRRLTITLEVEPSDTIENVKAKIQDK EGIPPDQQRLIFFGQQLEDGRTLSDYNIVKYSTLHLILRLNSWY
Water and common crystallization additives (CL, NA) are not listed.
Potent and selective inhibition of pathogenic viruses by engineered ubiquitin variants. Zhang, W., Bailey-Elkin, B.A., Knaap, R.C.M. et al. PLoS Pathog (2017) 13:e1006372-e1006372. DOI 10.1371/journal.ppat.1006372 · PubMed
Other PDB entries of the same protein (UniProt K0BWD0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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