Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants. Determined by X-ray diffraction at 1.65 Å resolution. Released 28 Jun 2002.
Explore 1KFN in 3D Show helices and sheets RCSB PDB PDBe
1KFN 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 | 2-49 | 48 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Major outer membrane lipoprotein | A | protein | 56 | Escherichia coli | P69776 (AlphaFold model) |
>1KFN_1 MAJOR OUTER MEMBRANE LIPOPROTEIN (chains A) SSNAKIDQLSSDVQTLNAKVDQASNDANAARSDAQAAKDDAARANQRLDNMATKYR
Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants. Liu, J., Cao, W., Lu, M. J Mol Biol (2002) 318:877-888. DOI 10.1016/S0022-2836(02)00138-9 · 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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