Research workbench
AlphaFold monomer V2.0 prediction for tripeptidyl-peptidase 1 (Q9XSB8)
Analyse AlphaFold monomer V2.0 prediction for tripeptidyl-peptidase 1 (Q9XSB8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9XSB8
- Type
- protein
- Length
- 563 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb0a2D657Af3Ac4FC3c0675DF7FC17dA77615d32E
- Molecule
- Tripeptidyl-peptidase 1
- UniProt
- Q9XSB8
- Pockets
- 5 · best druggability 0.72
Structure
1 distinct chain · 28% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tripeptidyl-peptidase 1 | protein | 563 | 28% helix, 23% strand | Q9XSB8 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 825 | 0.72 | 0.77 | 74 | empty |
| 2 | 70 | 0.65 | 0.93 | 23 | empty |
| 3 | 56 | 0.58 | 0.90 | 16 | empty |
| 4 | 136 | 0.41 | 0.75 | 18 | empty |
| 5 | 63 | 0.28 | 0.74 | 15 | empty |
Modifications
Observed in the structure: 3 disulfide (disulfide).
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 Q9XSB8
- Elsewhere: UniProt Q9XSB8 · AlphaFold DB Q9XSB8
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