Research workbench
Co-translational folding intermediate dictates membrane targeting of the signal recognition particle (SRP)- receptor
Analyse Co-translational folding intermediate dictates membrane targeting of the signal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FPK
- Type
- protein
- Length
- 53 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.95
- Source
- Escherichia coli (strain K12)
- Molecule
- Signal recognition particle receptor FtsY
- UniProt
- P10121
Structure
x-ray diffraction · resolution 1.95 · 1 distinct chain · 96% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Signal recognition particle receptor FtsY | protein | 53 | 96% helix, 0% strand | P10121 |
Ligands and binding sites
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6FPK · Co-translational folding intermediate dictates membrane targeting of the signal… · the same entry in another collection · chain A against A, TM-score 1.00
- P10121 · AlphaFold monomer V2.0 prediction for signal recognition particle receptor ftsy (P10121) · a predicted model of the same protein · chain A against A, TM-score 0.52
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P10121
- Elsewhere: RCSB PDB 6FPK · PDBe 6FPK · UniProt P10121
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