Multiple conformations in the ligand-binding site of the yeast nuclear pore targeting domain of NUP116P. Determined by solution NMR. Released 16 Aug 2005.
Explore 2AIV in 3D Show helices and sheets RCSB PDB PDBe
2AIV contains 4 α-helices and 10 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 | 7 | 1 | 1 |
| α-helix | 12-16 | 5 | |
| α-helix | 20-24 | 5 | |
| β-strand | 29-32 | 4 | 1 |
| β-strand | 38-41 | 4 | 1 |
| α-helix | 52-55 | 4 | |
| β-strand | 61-62 | 2 | 2 |
| β-strand | 67-68 | 2 | 2 |
| β-strand | 87-91 | 5 | 1 |
| β-strand | 98 | 1 | 3 |
| β-strand | 103 | 1 | 3 |
| α-helix | 113-122 | 10 | |
| β-strand | 127-131 | 5 | 1 |
| β-strand | 138-141 | 4 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| fragment of Nucleoporin NUP116/NSP116 | A | protein | 149 | Saccharomyces cerevisiae | Q02630 (AlphaFold model) |
>2AIV_1 fragment of Nucleoporin NUP116/NSP116 (chains A) GPNENYYISPSLDTLSSYSLLQLRKVPHLVVGHKSYGKIEFLEPVDLAGIPLTSLGGVII TFEPKTCIIYANLPNRPKRGEGINVRARITCFNCYPVDKSTRKPIKDPNHQLVKRHIERL KKNPNSKFESYDADSGTYVFIVNHAAEQT
Multiple Conformations in the Ligand-binding Site of the Yeast Nuclear Pore-targeting Domain of Nup116p. Robinson, M.A., Park, S., Sun, Z.-Y.J. et al. J Biol Chem (2005) 280:35723-35732. DOI 10.1074/jbc.M505068200 · PubMed
Other PDB entries of the same protein (UniProt Q02630 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2AIV 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.