Aminotryptophan Barstar. Determined by X-ray diffraction at 2.0 Å resolution. Released 22 Aug 2006.
Explore 2HXX in 3D Show helices and sheets RCSB PDB PDBe
2HXX contains 9 α-helices and 6 β-strands across 2 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 |
|---|---|---|---|
| β-strand | 2-6 | 5 | 1 |
| α-helix | 7-9 | 3 | |
| α-helix | 13-23 | 11 | |
| α-helix | 34-43 | 10 | |
| β-strand | 49-54 | 6 | 1 |
| α-helix | 56-61 | 6 | |
| α-helix | 66-79 | 14 | |
| β-strand | 84-88 | 5 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 1 |
| α-helix | 7-9 | 3 | |
| α-helix | 13-24 | 12 | |
| α-helix | 34-43 | 10 | |
| β-strand | 49-54 | 6 | 1 |
| α-helix | 68-79 | 12 | |
| β-strand | 84-88 | 5 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Barstar | A, B | protein | 89 | Bacillus amyloliquefaciens | P11540 (AlphaFold model) |
>2HXX_1 Barstar (chains A, B) KKAVINGEQIRSISDLHQTLKKELALAEYYGENLDALWDALTGWVEYPLVLEWRQFEQSK QLTENGAESVLQVFREAKAEGADITIILS
Aminotryptophan-containing barstar. Rubini, M., Lepthien, S., Golbik, R. et al. Biochim Biophys Acta (2006) 1764:1147-1158. DOI 10.1016/j.bbapap.2006.04.012 · PubMed
Other PDB entries of the same protein (UniProt P11540 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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