NMR solution structure of vMIP-II 1-71 from Kaposi's sarcoma-associated herpesvirus (minimized average structure). Determined by solution NMR. Released 7 Jan 2001.
Explore 1HFG in 3D Show helices and sheets RCSB PDB PDBe
1HFG contains 3 α-helices and 3 β-strands across 1 chain. 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 | 4-6 | 3 | |
| α-helix | 19-21 | 3 | |
| β-strand | 27-30 | 4 | 1 |
| β-strand | 40-43 | 4 | 1 |
| β-strand | 49-52 | 4 | 1 |
| α-helix | 58-65 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Viral macrophage inflammatory protein-II | A | protein | 71 | HUMAN HERPESVIRUS 8 | Q98157 (AlphaFold model) |
>1HFG_1 VIRAL MACROPHAGE INFLAMMATORY PROTEIN-II (chains A) LGASWHRPDKCCLGYQKRPLPQVLLSSWYPTSQLCSKPGVIFLTKRGRQVCADKSKDWVK KLMQQLPVTAR
Structure/Function of Human Herpesvirus-8 Mip-II (1-71) and the Antagonist N-Terminal Segment (1-10). Crump, M.P., Elisseeva, E., Gong, J.-H. et al. FEBS Lett (2001) 489:171. DOI 10.1016/S0014-5793(00)02393-0 · PubMed
Other PDB entries of the same protein (UniProt Q98157 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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