Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (B4EUF6)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (B4EUF6) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B4EUF6
- Type
- protein
- Length
- 545 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa2a8313a9ac1C6C2Fd647eb71D26A934AC647886
- Molecule
- CTP synthase
- UniProt
- B4EUF6
- Pockets
- 7 · best druggability 0.72
Structure
1 distinct chain · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 545 | 41% helix, 23% strand | B4EUF6 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 79 | 0.72 | 0.95 | 17 | empty |
| 2 | 280 | 0.53 | 0.75 | 37 | empty |
| 3 | 140 | 0.49 | 0.79 | 21 | empty |
| 4 | 111 | 0.41 | 0.76 | 25 | empty |
| 5 | 90 | 0.33 | 0.74 | 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 B4EUF6
- Elsewhere: UniProt B4EUF6 · AlphaFold DB B4EUF6
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