Research workbench
AlphaFold monomer V2.0 prediction for signal recognition particle receptor ftsy (P27414)
Analyse AlphaFold monomer V2.0 prediction for signal recognition particle receptor ftsy… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P27414
- Type
- protein
- Length
- 369 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb3c0C983Fc44934AC589D7131C08a72544EBB92E
- UniProt
- P27414
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 369 | — | P27414 |
Compared structures
- 5L3S · Structure of the GTPase heterodimer of crenarchaeal SRP54 and ftsy · an experimental structure of the same protein · chain A against B, TM-score 0.64
- 5L3S · Structure of the GTPase heterodimer of crenarchaeal SRP54 and FtsY · an experimental structure of the same protein · chain A against B, TM-score 0.64
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 P27414
- Elsewhere: UniProt P27414 · AlphaFold DB P27414
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