Research workbench
AlphaFold monomer V2.0 prediction for flavin-dependent thymidylate synthase (C5CHB8)
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
- C5CHB8
- Type
- protein
- Length
- 230 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7a1388B6Aad67B04634A32f63b8A6D6005eab86c
- Molecule
- Flavin-dependent thymidylate synthase
- UniProt
- C5CHB8
- Pockets
- 2 · best druggability 0.33
Structure
1 distinct chain · 47% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flavin-dependent thymidylate synthase | protein | 230 | 47% helix, 19% strand | C5CHB8 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.33 | 0.74 | 14 | empty |
| 2 | 59 | 0.30 | 0.75 | 16 | 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 C5CHB8
- Elsewhere: UniProt C5CHB8 · AlphaFold DB C5CHB8
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