Research workbench
AlphaFold monomer V2.0 prediction for flavin-dependent thymidylate synthase (A5U6A7)
Analyse AlphaFold monomer V2.0 prediction for flavin-dependent thymidylate synthase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5U6A7
- Type
- protein
- Length
- 250 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9466f3aB9A9154Ed7ca7fde206640ac62A405537
- Molecule
- Flavin-dependent thymidylate synthase
- UniProt
- A5U6A7
- Pockets
- 1 · best druggability 0.44
Structure
1 distinct chain · 46% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flavin-dependent thymidylate synthase | protein | 250 | 46% helix, 17% strand | A5U6A7 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 103 | 0.44 | 0.78 | 21 | 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 A5U6A7
- Elsewhere: UniProt A5U6A7 · AlphaFold DB A5U6A7
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