Barnase mutant with ile 88 replaced by ala. Determined by X-ray diffraction at 2.0 Å resolution. Released 10 Jul 1995.
Explore 1BRJ in 3D Show helices and sheets RCSB PDB PDBe
1BRJ contains 13 α-helices and 21 β-strands across 3 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 | 7-17 | 11 | |
| β-strand | 24-25 | 2 | 1 |
| α-helix | 27-32 | 6 | |
| α-helix | 37-39 | 3 | |
| α-helix | 42-45 | 4 | |
| β-strand | 50-51 | 2 | 1 |
| β-strand | 52-55 | 4 | 2 |
| α-helix | 64-65 | 2 | |
| β-strand | 71-75 | 5 | 2 |
| β-strand | 87-91 | 5 | 2 |
| β-strand | 96-99 | 4 | 2 |
| β-strand | 107-108 | 2 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-17 | 11 | |
| β-strand | 24-25 | 2 | 3 |
| α-helix | 27-32 | 6 | |
| α-helix | 37-39 | 3 | |
| α-helix | 42-45 | 4 | |
| β-strand | 50-51 | 2 | 3 |
| β-strand | 52-56 | 5 | 4 |
| β-strand | 71-75 | 5 | 4 |
| β-strand | 87-91 | 5 | 4 |
| β-strand | 96-99 | 4 | 4 |
| β-strand | 107-108 | 2 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Barnase | A, B, C | protein | 110 | Bacillus amyloliquefaciens | P00648 (AlphaFold model) |
>1BRJ_1 BARNASE (chains A, B, C) AQVINTFDGVADYLQTYHKLPDNYITKSEAQALGWVASKGNLADVAPGKSIGGDIFSNRE GKLPGKSGRTWREADINYTSGFRNSDRALYSSDWLIYKTTDHYQTFTKIR
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 1 |
Structural and energetic responses to cavity-creating mutations in hydrophobic cores: observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities. Buckle, A.M., Cramer, P., Fersht, A.R. Biochemistry (1996) 35:4298-4305. DOI 10.1021/bi9524676 · PubMed
Other PDB entries of the same protein (UniProt P00648 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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