Barstar (FREE), C82A mutant. Determined by X-ray diffraction at 2.76 Å resolution. Released 8 Apr 1998.
Explore 1A19 in 3D Show helices and sheets RCSB PDB PDBe
1A19 contains 10 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 | 13-23 | 11 | |
| α-helix | 34-39 | 6 | |
| α-helix | 40-44 | 5 | |
| α-helix | 46 | 1 | |
| β-strand | 49-54 | 6 | 1 |
| α-helix | 56-61 | 6 | |
| α-helix | 67-80 | 14 | |
| β-strand | 84-88 | 5 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 1 |
| α-helix | 13-23 | 11 | |
| α-helix | 34-41 | 8 | |
| β-strand | 49-54 | 6 | 1 |
| α-helix | 56-61 | 6 | |
| α-helix | 67-80 | 14 | |
| β-strand | 84-88 | 5 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Barstar | A, B | protein | 90 | Bacillus amyloliquefaciens | P11540 (AlphaFold model) |
>1A19_1 BARSTAR (chains A, B) MKKAVINGEQIRSISDLHQTLKKELALPEYYGENLDALWDCLTGWVEYPLVLEWRQFEQS KQLTENGAESVLQVFREAKAEGADITIILS
Discrepancies between the NMR and X-ray structures of uncomplexed barstar: analysis suggests that packing densities of protein structures determined by NMR are unreliable. Ratnaparkhi, G.S., Ramachandran, S., Udgaonkar, J.B. et al. Biochemistry (1998) 37:6958-6966. DOI 10.1021/bi972857n · PubMed
Other PDB entries of the same protein (UniProt P11540 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1A19 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.