Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (A4FKA9)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (A4FKA9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4FKA9
- Type
- protein
- Length
- 568 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4450b8770f8579152a0dD84fBd7622763A5eC221
- Molecule
- CTP synthase
- UniProt
- A4FKA9
- Pockets
- 5 · best druggability 0.73
Structure
1 distinct chain · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 568 | 42% helix, 21% strand | A4FKA9 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 267 | 0.73 | 0.87 | 41 | empty |
| 2 | 286 | 0.54 | 0.75 | 34 | empty |
| 3 | 142 | 0.53 | 0.81 | 19 | empty |
| 4 | 65 | 0.33 | 0.76 | 13 | empty |
| 5 | 60 | 0.30 | 0.76 | 13 | 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 A4FKA9
- Elsewhere: UniProt A4FKA9 · AlphaFold DB A4FKA9
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