Solution structure of virus chemokine vmip-II. Determined by solution NMR. Released 16 Sept 2003.
Explore 1HHV in 3D Show helices and sheets RCSB PDB PDBe
1HHV contains 1 α-helix and 4 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 |
|---|---|---|---|
| β-strand | 30-33 | 4 | 1 |
| β-strand | 43-46 | 4 | 1 |
| β-strand | 52-55 | 4 | 1 |
| α-helix | 60-68 | 9 | |
| β-strand | 71 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Virus chemokine vmip-II | A | protein | 74 | Q98157 (AlphaFold model) |
>1HHV_1 VIRUS CHEMOKINE VMIP-II (chains A) GDTLGASWHRPDKCCLGYQKRPLPQVLLSSWYPTSQLCSKPGVIFLTKRGRQVCADKSKD WVKKLMQQLPVTAR
CCR2 and CCR5 receptor-binding properties of herpesvirus-8 vMIP-II based on sequence analysis and its solution structure. Shao, W., Fernandez, E., Sachpatzidis, A. et al. Eur J Biochem (2001) 268:2948-2959. DOI 10.1046/j.1432-1327.2001.02184.x · 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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