Solution structure of the yeast Sti1 DP1 domain. Determined by solution NMR. Released 25 Jan 2012.
Explore 2LLV in 3D Show helices and sheets RCSB PDB PDBe
2LLV contains 6 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 | 133-137 | 5 | |
| α-helix | 142-147 | 6 | |
| α-helix | 152-156 | 5 | |
| α-helix | 160-169 | 10 | |
| α-helix | 174-177 | 4 | |
| α-helix | 182-192 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Heat shock protein STI1 | A | protein | 71 | Saccharomyces cerevisiae | P15705 (AlphaFold model) |
>2LLV_1 Heat shock protein STI1 (chains A) QPDLGLTQLFADPNLIENLKKNPKTSEMMKDPQLVAKLIGYKQNPQAIGQDLFTDPRLMT IMATLMGVDLN
The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop. Schmid, A.B., Lagleder, S., Grawert, M.A. et al. EMBO J (2012) 31:1506-1517. DOI 10.1038/emboj.2011.472 · PubMed
Other PDB entries of the same protein (UniProt P15705 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2LLV 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.