MolNFT v1 · #471567 · protein
AlphaFold monomer V2.0 prediction for tripeptidyl-peptidase 1 (Q55CT0)
Q55CT0: “AlphaFold monomer V2.0 prediction for tripeptidyl-peptidase 1 (Q55CT0)”. 7 pockets (best druggability 0.70). MolNFT v1 #471567 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q55CT0
- Type
- protein
- Length
- 600 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x025f3b1a898b05AD2731bE6Ab72687b5920c4A3F
- Molecule
- Tripeptidyl-peptidase 1
- UniProt
- Q55CT0
- Pockets
- 7 · best druggability 0.70
Structure
1 distinct chain · 29% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tripeptidyl-peptidase 1 | protein | 600 | 29% helix, 20% strand | Q55CT0 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 439 | 0.70 | 0.81 | 53 | empty |
| 2 | 129 | 0.48 | 0.79 | 27 | empty |
| 3 | 133 | 0.45 | 0.77 | 34 | empty |
| 4 | 137 | 0.44 | 0.77 | 27 | empty |
| 5 | 99 | 0.40 | 0.77 | 18 | empty |
Modifications
Observed in the structure: 1 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 Q55CT0
- Elsewhere: UniProt Q55CT0 · AlphaFold DB Q55CT0
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