Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (B5EPM5)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (B5EPM5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5EPM5
- Type
- protein
- Length
- 545 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA0f5ea066576302D69daD07dD048eA72B2b46B7e
- Molecule
- CTP synthase
- UniProt
- B5EPM5
- Pockets
- 6 · best druggability 0.68
Structure
1 distinct chain · 40% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 545 | 40% helix, 23% strand | B5EPM5 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 131 | 0.68 | 0.89 | 26 | empty |
| 2 | 263 | 0.54 | 0.76 | 39 | empty |
| 3 | 139 | 0.43 | 0.75 | 25 | empty |
| 4 | 90 | 0.41 | 0.78 | 26 | empty |
| 5 | 103 | 0.38 | 0.75 | 24 | 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 B5EPM5
- Elsewhere: UniProt B5EPM5 · AlphaFold DB B5EPM5
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