Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (Q4FM39)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (Q4FM39) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q4FM39
- Type
- protein
- Length
- 538 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd91633319BDB0a92cbC4f08DeA734Bf74C030064
- Molecule
- CTP synthase
- UniProt
- Q4FM39
- Pockets
- 4 · best druggability 0.66
Structure
1 distinct chain · 41% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 538 | 41% helix, 24% strand | Q4FM39 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 172 | 0.66 | 0.86 | 24 | empty |
| 2 | 321 | 0.55 | 0.75 | 38 | empty |
| 3 | 186 | 0.47 | 0.75 | 22 | empty |
| 4 | 131 | 0.47 | 0.78 | 26 | 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 Q4FM39
- Elsewhere: UniProt Q4FM39 · AlphaFold DB Q4FM39
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