Co-translational folding intermediate dictates membrane targeting of the signal recognition particle (SRP)- receptor. Determined by X-ray diffraction at 2.65 Å resolution. Released 9 May 2018.
Explore 6FPR in 3D Show helices and sheets RCSB PDB PDBe
6FPR contains 2 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 7-51 | 45 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-60 | 53 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Signal recognition particle receptor FtsY | A, B | protein | 62 | Escherichia coli (strain K12) | P10121 (AlphaFold model) |
>6FPR_1 Signal recognition particle receptor FtsY (chains A, B) GSKKIDDDLFEELEEQLLIADVGVETTRKIITNLTEGASRKQLRDAEALYGLLKEEMGEI LA
Co-translational Folding Intermediate Dictates Membrane Targeting of the Signal Recognition Particle Receptor. Karniel, A., Mrusek, D., Steinchen, W. et al. J Mol Biol (2018) 430:1607-1620. DOI 10.1016/j.jmb.2018.04.017 · PubMed
Other PDB entries of the same protein (UniProt P10121 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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