Cryo-EM Structure of KSHV ORF74 Apo Dimer at 2.8A. Determined by electron microscopy at 2.89 Å resolution. Released 27 Aug 2025.
Explore 8W1A in 3D Show helices and sheets RCSB PDB PDBe
8W1A contains 32 α-helices and 4 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 |
|---|---|---|---|
| α-helix | 47-74 | 28 | |
| α-helix | 76-78 | 3 | |
| α-helix | 81-108 | 28 | |
| α-helix | 110-112 | 3 | |
| α-helix | 115-148 | 34 | |
| α-helix | 154-156 | 3 | |
| α-helix | 158-179 | 22 | |
| β-strand | 184-187 | 4 | 1 |
| β-strand | 194-197 | 4 | 1 |
| α-helix | 201-203 | 3 | |
| α-helix | 204-216 | 13 | |
| α-helix | 217-221 | 5 | |
| α-helix | 222-241 | 20 | |
| α-helix | 251-263 | 13 | |
| α-helix | 265-278 | 14 | |
| α-helix | 286-317 | 32 | |
| α-helix | 319-329 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 39-41 | 3 | |
| α-helix | 47-73 | 27 | |
| α-helix | 76-78 | 3 | |
| α-helix | 81-108 | 28 | |
| α-helix | 110-112 | 3 | |
| α-helix | 115-148 | 34 | |
| α-helix | 154-156 | 3 | |
| α-helix | 158-179 | 22 | |
| β-strand | 184-187 | 4 | 2 |
| β-strand | 194-197 | 4 | 2 |
| α-helix | 201-203 | 3 | |
| α-helix | 204-216 | 13 | |
| α-helix | 217-221 | 5 | |
| α-helix | 222-240 | 19 | |
| α-helix | 247-249 | 3 | |
| α-helix | 251-263 | 13 | |
| α-helix | 265-278 | 14 | |
| α-helix | 286-316 | 31 | |
| α-helix | 319-330 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| viral G-protein coupled receptor | A, B | protein | 369 | Human gammaherpesvirus 8 | Q98146 (AlphaFold model) |
>8W1A_1 viral G-protein coupled receptor (chains A, B) MAAEDFLTIFLDDDESWNETLNMSGYDYSGNFSLEVSVCEMTTVVPYTWNVGILSLIFLI NVLGNGLVTYIFCKHRSRAGAIDILLLGICLNSLCLSISLLAEVLMFLFPNIISTGLCRL EIFFYYLYVYLDIFSVVCVSLVRYLLVAYSTRSWPKKQSLGWVLTSAAWLIALVLSGDAC RHRSRVVDPVSKQAMCYENAGNMTADWRLHVRTVSVTAGFLLPLALLILFYALTWCVVRR TKLQARRKVRGVIVAVVVLFFVFCFPYHVLNLLDTLLRRRWIRDSCYTRGLINVGLAVTS LLQALYSAVVPLIYSCLGSLFRQRMYGLFQSLRQSFMSGADYKDDDDKGRPLEVLFQGPH HHHHHHHHH
Structural basis for ligand promiscuity and high signaling activity of Kaposi's Sarcoma-associated Herpesvirus-encoded GPCR. Park, J.B., Sahoo, B., Sahoo, A.R. et al. Nat Commun (2025) 16:8403-8403. DOI 10.1038/s41467-025-63457-4 · PubMed
Other PDB entries of the same protein (UniProt Q98146 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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