Research workbench
AlphaFold monomer V2.0 prediction for signal recognition particle 54 kda protein (Q9HMN5)
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
- Q9HMN5
- Type
- protein
- Length
- 460 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf87a97E0A4bB354D834857B14296240B167cbe70
- Molecule
- Signal recognition particle 54 kda protein
- UniProt
- Q9HMN5
- Pockets
- 5 · best druggability 0.76
Structure
1 distinct chain · 57% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Signal recognition particle 54 kda protein | protein | 460 | 57% helix, 9% strand | Q9HMN5 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 294 | 0.76 | 0.88 | 40 | empty |
| 2 | 160 | 0.44 | 0.75 | 22 | empty |
| 3 | 76 | 0.37 | 0.77 | 18 | empty |
| 4 | 54 | 0.30 | 0.76 | 18 | empty |
| 5 | 56 | 0.27 | 0.74 | 11 | 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 Q9HMN5
- Elsewhere: UniProt Q9HMN5 · AlphaFold DB Q9HMN5
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