Research workbench
AlphaFold monomer V2.0 prediction for tripeptidyl-peptidase 2 (P29144)
Analyse AlphaFold monomer V2.0 prediction for tripeptidyl-peptidase 2 (P29144) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P29144
- Type
- protein
- Length
- 1,249 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc0F878C3f3E2a1874e2A6daC80d429e553DdB0D5
- Molecule
- Tripeptidyl-peptidase 2
- UniProt
- P29144
- Pockets
- 13 · best druggability 0.78
Structure
1 distinct chain · 32% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tripeptidyl-peptidase 2 | protein | 1249 | 32% helix, 30% strand | P29144 |
Pockets
13 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 488 | 0.78 | 0.86 | 57 | empty |
| 2 | 544 | 0.73 | 0.81 | 56 | empty |
| 3 | 432 | 0.66 | 0.78 | 38 | empty |
| 4 | 208 | 0.52 | 0.77 | 28 | empty |
| 5 | 116 | 0.41 | 0.75 | 23 | 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 P29144
- Elsewhere: UniProt P29144 · AlphaFold DB P29144
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