Research workbench
AlphaFold monomer V2.0 prediction for tripeptidyl-peptidase SED1 (C5FHK0)
Analyse AlphaFold monomer V2.0 prediction for tripeptidyl-peptidase SED1 (C5FHK0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C5FHK0
- Type
- protein
- Length
- 670 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd27f4D98eE625C1f8E81f7ac0eF38f876f24543e
- Molecule
- Tripeptidyl-peptidase SED1
- UniProt
- C5FHK0
- Pockets
- 6 · best druggability 0.85
Structure
1 distinct chain · 25% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tripeptidyl-peptidase SED1 | protein | 670 | 25% helix, 22% strand | C5FHK0 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 961 | 0.85 | 0.86 | 95 | empty |
| 2 | 438 | 0.58 | 0.74 | 40 | empty |
| 3 | 161 | 0.49 | 0.77 | 37 | empty |
| 4 | 136 | 0.43 | 0.76 | 24 | empty |
| 5 | 54 | 0.36 | 0.80 | 17 | empty |
Modifications
Observed in the structure: 4 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 C5FHK0
- Elsewhere: UniProt C5FHK0 · AlphaFold DB C5FHK0
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