Crystal structure of the B30.2/SPRY domain of GUSTAVUS in complex with a 20-residue VASA peptide. Determined by X-ray diffraction at 2.2 Å resolution. Released 16 Jan 2007.
Explore 2IHS in 3D Show helices and sheets RCSB PDB PDBe
2IHS contains 11 α-helices and 40 β-strands across 4 chains. 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 | 39-46 | 8 | |
| α-helix | 48-51 | 4 | |
| α-helix | 52-57 | 6 | |
| β-strand | 60-65 | 6 | 1 |
| β-strand | 69-71 | 3 | 2 |
| β-strand | 78-81 | 4 | 2 |
| β-strand | 84 | 1 | 3 |
| β-strand | 87-93 | 7 | 1 |
| β-strand | 97 | 1 | 4 |
| β-strand | 101-107 | 7 | 2 |
| α-helix | 110-112 | 3 | |
| β-strand | 118-122 | 5 | 1 |
| β-strand | 129-131 | 3 | 1 |
| β-strand | 143-147 | 5 | 1 |
| β-strand | 152-155 | 4 | 1 |
| β-strand | 160 | 1 | 5 |
| β-strand | 163-164 | 2 | 1 |
| α-helix | 167-168 | 2 | |
| β-strand | 180-186 | 7 | 2 |
| β-strand | 191-196 | 6 | 2 |
| β-strand | 199-206 | 8 | 2 |
| β-strand | 213 | 1 | 4 |
| β-strand | 214-219 | 6 | 1 |
| β-strand | 225-234 | 10 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 39-46 | 8 | |
| α-helix | 48-50 | 3 | |
| α-helix | 52-57 | 6 | |
| β-strand | 60-65 | 6 | 6 |
| β-strand | 69-72 | 4 | 7 |
| β-strand | 75-81 | 7 | 7 |
| β-strand | 84 | 1 | 8 |
| β-strand | 87-93 | 7 | 6 |
| β-strand | 97 | 1 | 9 |
| β-strand | 101-107 | 7 | 7 |
| α-helix | 110-112 | 3 | |
| β-strand | 118-122 | 5 | 6 |
| β-strand | 129-131 | 3 | 6 |
| β-strand | 143-147 | 5 | 6 |
| β-strand | 152-155 | 4 | 6 |
| β-strand | 160 | 1 | 5 |
| β-strand | 163-164 | 2 | 6 |
| α-helix | 167-168 | 2 | |
| β-strand | 180-186 | 7 | 7 |
| β-strand | 191-195 | 5 | 7 |
| β-strand | 200-205 | 6 | 7 |
| β-strand | 213 | 1 | 9 |
| β-strand | 214-219 | 6 | 6 |
| β-strand | 225-233 | 9 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 189 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 189 | 1 | 8 |
| α-helix | 195-199 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CG2944-PF, isoform F | A, B | protein | 214 | Drosophila melanogaster | A1Z6E0 (AlphaFold model) |
| 20-mer from ATP-dependent RNA helicase vasa | C, D | protein | 20 | Drosophila melanogaster | P09052 (AlphaFold model) |
>2IHS_1 CG2944-PF, isoform F (chains A, B) GHMRELQADFVKPARIDILLDMPPASRDLQLKHSWNSEDRSLNIFVKEDDKLTFHRHPVA QSTDCIRGKVGLTKGLHIWEIYWPTRQRGTHAVVGVCTADAPLHSVGYQSLVGSTEQSWG WDLGRNKLYHDSKNCAGVTYPAILKNDEAFLVPDKFLVALDMDEGTLSFIVDQQYLGIAF RGLRGKKLYPIVSAVWGHCEITMRYIGGLVDELN
>2IHS_2 20-mer from ATP-dependent RNA helicase vasa (chains C, D) DINNNNNIVEDVERKREFYI
Structural Basis for Protein Recognition by B30.2/SPRY Domains. Woo, J.S., Suh, H.Y., Park, S.Y. et al. Mol Cell (2006) 24:967-976. DOI 10.1016/j.molcel.2006.11.009 · PubMed
Other PDB entries of the same protein (UniProt A1Z6E0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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