Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (A5FHA4)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (A5FHA4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5FHA4
- Type
- protein
- Length
- 537 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xe3E92b54e6Bc4ff98Bc361E0bA88a4CC998BcD4a
- Molecule
- CTP synthase
- UniProt
- A5FHA4
- Pockets
- 5 · best druggability 0.63
Structure
1 distinct chain · 42% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 537 | 42% helix, 22% strand | A5FHA4 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 151 | 0.63 | 0.85 | 36 | empty |
| 2 | 299 | 0.55 | 0.76 | 37 | empty |
| 3 | 105 | 0.37 | 0.74 | 20 | empty |
| 4 | 67 | 0.30 | 0.74 | 19 | empty |
| 5 | 56 | 0.28 | 0.74 | 16 | 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 A5FHA4
- Elsewhere: UniProt A5FHA4 · AlphaFold DB A5FHA4
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