Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (Q5L5S1)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (Q5L5S1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5L5S1
- Type
- protein
- Length
- 537 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa62D9E278a4a7e393ABAEF11f424ec107F27E47B
- Molecule
- CTP synthase
- UniProt
- Q5L5S1
- Pockets
- 4 · best druggability 0.65
Structure
1 distinct chain · 43% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 537 | 43% helix, 21% strand | Q5L5S1 |
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 | 146 | 0.65 | 0.87 | 28 | empty |
| 2 | 288 | 0.56 | 0.77 | 37 | empty |
| 3 | 194 | 0.46 | 0.74 | 25 | empty |
| 4 | 73 | 0.31 | 0.74 | 20 | 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 Q5L5S1
- Elsewhere: UniProt Q5L5S1 · AlphaFold DB Q5L5S1
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