Research workbench
AlphaFold monomer V2.0 prediction for probable tripeptidyl-peptidase SED2 (D4ANG0)
Analyse AlphaFold monomer V2.0 prediction for probable tripeptidyl-peptidase SED2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- D4ANG0
- Type
- protein
- Length
- 596 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7FDF8b382C6a36A8772D1A265E8e480c7DF0A9C1
- Molecule
- Probable tripeptidyl-peptidase SED2
- UniProt
- D4ANG0
- Pockets
- 5 · best druggability 0.68
Structure
1 distinct chain · 28% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable tripeptidyl-peptidase SED2 | protein | 596 | 28% helix, 22% strand | D4ANG0 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 163 | 0.68 | 0.88 | 37 | empty |
| 2 | 193 | 0.49 | 0.75 | 29 | empty |
| 3 | 72 | 0.46 | 0.82 | 16 | empty |
| 4 | 138 | 0.42 | 0.75 | 23 | empty |
| 5 | 53 | 0.30 | 0.75 | 14 | 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 D4ANG0
- Elsewhere: UniProt D4ANG0 · AlphaFold DB D4ANG0
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