Research workbench
AlphaFold monomer V2.0 prediction for xaa-pro dipeptidase (B4SI11)
Analyse AlphaFold monomer V2.0 prediction for xaa-pro dipeptidase (B4SI11) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B4SI11
- Type
- protein
- Length
- 443 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBF0D2e107Ce1EcD2C4369B042274201DB719AaAF
- Molecule
- Xaa-pro dipeptidase
- UniProt
- B4SI11
- Pockets
- 4 · best druggability 0.57
Structure
1 distinct chain · 40% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Xaa-pro dipeptidase | protein | 443 | 40% helix, 16% strand | B4SI11 |
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 | 362 | 0.57 | 0.75 | 48 | empty |
| 2 | 110 | 0.50 | 0.81 | 20 | empty |
| 3 | 68 | 0.34 | 0.76 | 17 | empty |
| 4 | 69 | 0.30 | 0.74 | 24 | 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 B4SI11
- Elsewhere: UniProt B4SI11 · AlphaFold DB B4SI11
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