Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (Q136D7)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (Q136D7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q136D7
- Type
- protein
- Length
- 543 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8af20c751cd561e3F0B6141F3317c17894026A1c
- Molecule
- CTP synthase
- UniProt
- Q136D7
- Pockets
- 5 · best druggability 0.72
Structure
1 distinct chain · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 543 | 41% helix, 23% strand | Q136D7 |
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 | 482 | 0.72 | 0.82 | 62 | empty |
| 2 | 267 | 0.52 | 0.75 | 29 | empty |
| 3 | 154 | 0.45 | 0.76 | 26 | empty |
| 4 | 146 | 0.45 | 0.76 | 19 | empty |
| 5 | 53 | 0.30 | 0.76 | 13 | 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 Q136D7
- Elsewhere: UniProt Q136D7 · AlphaFold DB Q136D7
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