Research workbench
AlphaFold monomer V2.0 prediction for signal recognition particle subunit SRP72 (P49965)
Analyse AlphaFold monomer V2.0 prediction for signal recognition particle subunit SRP72… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P49965
- Type
- protein
- Length
- 707 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x71112d4fF7ebb3b617963c05f052289e073082FD
- Molecule
- Signal recognition particle subunit SRP72
- UniProt
- P49965
- Pockets
- 4 · best druggability 0.71
Structure
1 distinct chain · 61% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Signal recognition particle subunit SRP72 | protein | 707 | 61% helix, 1% strand | P49965 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 828 | 0.71 | 0.77 | 56 | empty |
| 2 | 78 | 0.41 | 0.79 | 15 | empty |
| 3 | 56 | 0.31 | 0.76 | 12 | empty |
| 4 | 54 | 0.30 | 0.75 | 14 | 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 P49965
- Elsewhere: UniProt P49965 · AlphaFold DB P49965
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