Research workbench
AlphaFold monomer V2.0 prediction for xaa-pro dipeptidyl-peptidase (Q97RC8)
Analyse AlphaFold monomer V2.0 prediction for xaa-pro dipeptidyl-peptidase (Q97RC8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q97RC8
- Type
- protein
- Length
- 757 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x97EfFf2d74994e28D3b69b1503Bd9c292B2Df480
- Molecule
- Xaa-pro dipeptidyl-peptidase
- UniProt
- Q97RC8
- Pockets
- 7 · best druggability 0.54
Structure
1 distinct chain · 26% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Xaa-pro dipeptidyl-peptidase | protein | 757 | 26% helix, 28% strand | Q97RC8 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 245 | 0.54 | 0.77 | 25 | empty |
| 2 | 243 | 0.51 | 0.75 | 36 | empty |
| 3 | 223 | 0.50 | 0.75 | 34 | empty |
| 4 | 169 | 0.48 | 0.76 | 25 | empty |
| 5 | 56 | 0.44 | 0.83 | 20 | 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 Q97RC8
- Elsewhere: UniProt Q97RC8 · AlphaFold DB Q97RC8
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