Research workbench
AlphaFold monomer V2.0 prediction for chaperone protein tord (B5FME2)
Analyse AlphaFold monomer V2.0 prediction for chaperone protein tord (B5FME2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5FME2
- Type
- protein
- Length
- 210 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x71112d4fF7ebb3b617963c05f052289e073082FD
- Molecule
- Chaperone protein tord
- UniProt
- B5FME2
- Pockets
- 2 · best druggability 0.44
Structure
1 distinct chain · 66% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein tord | protein | 210 | 66% helix, 1% strand | B5FME2 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 168 | 0.44 | 0.75 | 24 | empty |
| 2 | 61 | 0.30 | 0.74 | 13 | 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 B5FME2
- Elsewhere: UniProt B5FME2 · AlphaFold DB B5FME2
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