Research workbench
AlphaFold monomer V2.0 prediction for signal recognition particle 54 kda protein (C5A233)
Analyse AlphaFold monomer V2.0 prediction for signal recognition particle 54 kda… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C5A233
- Type
- protein
- Length
- 448 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x025f3b1a898b05AD2731bE6Ab72687b5920c4A3F
- Molecule
- Signal recognition particle 54 kda protein
- UniProt
- C5A233
- Pockets
- 5 · best druggability 0.74
Structure
1 distinct chain · 59% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Signal recognition particle 54 kda protein | protein | 448 | 59% helix, 9% strand | C5A233 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 518 | 0.74 | 0.82 | 47 | empty |
| 2 | 337 | 0.55 | 0.74 | 39 | empty |
| 3 | 64 | 0.45 | 0.82 | 11 | empty |
| 4 | 59 | 0.33 | 0.77 | 11 | empty |
| 5 | 57 | 0.33 | 0.78 | 20 | empty |
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 C5A233
- Elsewhere: UniProt C5A233 · AlphaFold DB C5A233
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