Protection against experimental P. falciparum malaria is associated with short AMA-1 peptide analogue alpha-helical structures. Determined by solution NMR. Released 4 Feb 2015.
Explore 2MTX in 3D Show helices and sheets RCSB PDB PDBe
2MTX contains 2 α-helices and 0 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 | 13-16 | 4 | |
| α-helix | 17-19 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apical membrane antigen-1 | A | protein | 21 | Plasmodium falciparum | Q9BIM8 (AlphaFold model) |
>2MTX_1 Apical membrane antigen-1 (chains A) MIKSAFLPTGAFKADRYKSHX
Protection against experimental P. falciparum malaria is associated with short AMA-1 peptide analogue alpha-helical structures. Cubillos, M., Salazar, L., Torres, L. et al. To be published.
Other PDB entries of the same protein (UniProt Q9BIM8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2MTX directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.