Conformational Transition between Four- and Five-stranded Phenylalanine Zippers Determined by a Local Packing Interaction. Determined by X-ray diffraction at 1.75 Å resolution. Released 25 Jul 2006.
Explore 2GUS in 3D Show helices and sheets RCSB PDB PDBe
2GUS contains 1 α-helix and 0 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 |
|---|---|---|---|
| α-helix | 14-53 | 40 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Major outer membrane lipoprotein | A | protein | 56 | Escherichia coli | P69776 (AlphaFold model) |
>2GUS_1 Major outer membrane lipoprotein (chains A) SSNAKFDQFSSDFQTFNAKFDQFSNDMNAFRSDFQAFKDDFARFNQRFDNFATKYR
Conformational Transition between Four and Five-stranded Phenylalanine Zippers Determined by a Local Packing Interaction. Liu, J., Zheng, Q., Deng, Y. et al. J Mol Biol (2006) 361:168-179. DOI 10.1016/j.jmb.2006.05.063 · PubMed
Other PDB entries of the same protein (UniProt P69776 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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