Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (Q1MR71)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (Q1MR71) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1MR71
- Type
- protein
- Length
- 550 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd91633319BDB0a92cbC4f08DeA734Bf74C030064
- Molecule
- CTP synthase
- UniProt
- Q1MR71
- Pockets
- 7 · best druggability 0.66
Structure
1 distinct chain · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 550 | 41% helix, 23% strand | Q1MR71 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 170 | 0.66 | 0.86 | 28 | empty |
| 2 | 247 | 0.51 | 0.75 | 34 | empty |
| 3 | 125 | 0.47 | 0.78 | 19 | empty |
| 4 | 128 | 0.45 | 0.78 | 28 | empty |
| 5 | 117 | 0.42 | 0.76 | 17 | 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 Q1MR71
- Elsewhere: UniProt Q1MR71 · AlphaFold DB Q1MR71
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