NMR 15N relaxation and structural studies reveal conformational exchange in barstar C40/82A, 30 structures. Determined by solution NMR. Released 4 Sept 1997.
Explore 1AB7 in 3D Show helices and sheets RCSB PDB PDBe
1AB7 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 | 2-5 | 4 | 1 |
| α-helix | 13-20 | 8 | |
| α-helix | 21-25 | 5 | |
| α-helix | 34-41 | 8 | |
| β-strand | 49-53 | 5 | 1 |
| α-helix | 67-80 | 14 | |
| β-strand | 84-87 | 4 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Barstar | A | protein | 89 | Bacillus amyloliquefaciens | P11540 (AlphaFold model) |
>1AB7_1 BARSTAR (chains A) KKAVINGEQIRSISDLHQTLKKELALPEYYGENLDALWDALTGWVEYPLVLEWRQFEQSK QLTENGAESVLQVFREAKAEGADITIILS
NMR 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A. Wong, K.B., Fersht, A.R., Freund, S.M. J Mol Biol (1997) 268:494-511. DOI 10.1006/jmbi.1997.0989 · 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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