Three-dimensional solution structure and 13C assignments of barstar using nuclear magnetic resonance spectroscopy. Determined by solution NMR. Released 31 Jul 1994.
Explore 1BTA in 3D Show helices and sheets RCSB PDB PDBe
1BTA contains 4 α-helices and 3 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 | 2-6 | 5 | 1 |
| α-helix | 13-24 | 12 | |
| α-helix | 34-41 | 8 | |
| β-strand | 49-54 | 6 | 1 |
| α-helix | 58-61 | 4 | |
| α-helix | 67-79 | 13 | |
| β-strand | 84-88 | 5 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Barstar | A | protein | 89 | Bacillus amyloliquefaciens | P11540 (AlphaFold model) |
>1BTA_1 BARSTAR (chains A) KKAVINGEQIRSISDLHQTLKKELALPEYYGENLDALWDCLTGWVEYPLVLEWRQFEQSK QLTENGAESVLQVFREAKAEGCDITIILS
Three-dimensional solution structure and 13C assignments of barstar using nuclear magnetic resonance spectroscopy. Lubienski, M.J., Bycroft, M., Freund, S.M. et al. Biochemistry (1994) 33:8866-8877. DOI 10.1021/bi00196a003 · PubMed
Other PDB entries of the same protein (UniProt P11540 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1BTA 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.