Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (B4RJ40)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (B4RJ40) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B4RJ40
- Type
- protein
- Length
- 544 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x00015c671bd119DC86Baf28AF2eB830022fb46C1
- Molecule
- CTP synthase
- UniProt
- B4RJ40
- Pockets
- 5 · best druggability 0.65
Structure
1 distinct chain · 41% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 544 | 41% helix, 24% strand | B4RJ40 |
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 | 141 | 0.65 | 0.87 | 28 | empty |
| 2 | 396 | 0.60 | 0.76 | 48 | empty |
| 3 | 129 | 0.46 | 0.78 | 35 | empty |
| 4 | 100 | 0.36 | 0.75 | 23 | empty |
| 5 | 59 | 0.32 | 0.76 | 14 | 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 B4RJ40
- Elsewhere: UniProt B4RJ40 · AlphaFold DB B4RJ40
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