Research workbench
AlphaFold monomer V2.0 prediction for dipeptidyl-peptidase 5 (Q9P778)
Analyse AlphaFold monomer V2.0 prediction for dipeptidyl-peptidase 5 (Q9P778) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9P778
- Type
- protein
- Length
- 683 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5e58272ea25a05e06901A2eAe9f63939b344e0c6
- Molecule
- Dipeptidyl-peptidase 5
- UniProt
- Q9P778
- Pockets
- 4 · best druggability 0.78
Structure
1 distinct chain · 18% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dipeptidyl-peptidase 5 | protein | 683 | 18% helix, 37% strand | Q9P778 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 993 | 0.78 | 0.80 | 97 | empty |
| 2 | 655 | 0.74 | 0.80 | 50 | empty |
| 3 | 327 | 0.60 | 0.77 | 35 | empty |
| 4 | 57 | 0.33 | 0.77 | 19 | 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 Q9P778
- Elsewhere: UniProt Q9P778 · AlphaFold DB Q9P778
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