Research workbench
AlphaFold monomer V2.0 prediction for signal recognition particle SEC65 subunit (P41922)
Analyse AlphaFold monomer V2.0 prediction for signal recognition particle SEC65 subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P41922
- Type
- protein
- Length
- 310 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x78Cc7f9BF18AF8279e492D45EE7Fe9d7cC6f6D07
- Molecule
- Signal recognition particle SEC65 subunit
- UniProt
- P41922
- Pockets
- 4 · best druggability 0.41
Structure
1 distinct chain · 31% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Signal recognition particle SEC65 subunit | protein | 310 | 31% helix, 5% strand | P41922 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 117 | 0.41 | 0.75 | 19 | empty |
| 2 | 97 | 0.37 | 0.75 | 14 | empty |
| 3 | 60 | 0.32 | 0.75 | 14 | empty |
| 4 | 51 | 0.29 | 0.75 | 18 | 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 P41922
- Elsewhere: UniProt P41922 · AlphaFold DB P41922
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