Research workbench
AlphaFold monomer V2.0 prediction for xaa-pro dipeptidase (Q8FBI1)
Analyse AlphaFold monomer V2.0 prediction for xaa-pro dipeptidase (Q8FBI1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8FBI1
- Type
- protein
- Length
- 443 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbff27Dc0a932A6E0d9Fe883AAbD1BF27bB95A69F
- Molecule
- Xaa-pro dipeptidase
- UniProt
- Q8FBI1
- Pockets
- 5 · best druggability 0.55
Structure
1 distinct chain · 37% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Xaa-pro dipeptidase | protein | 443 | 37% helix, 17% strand | Q8FBI1 |
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 | 150 | 0.55 | 0.81 | 25 | empty |
| 2 | 74 | 0.38 | 0.78 | 16 | empty |
| 3 | 53 | 0.33 | 0.78 | 16 | empty |
| 4 | 66 | 0.32 | 0.75 | 14 | empty |
| 5 | 62 | 0.29 | 0.74 | 15 | 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 Q8FBI1
- Elsewhere: UniProt Q8FBI1 · AlphaFold DB Q8FBI1
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