Research workbench
AlphaFold monomer V2.0 prediction for tRNA-modifying protein ygfz (C3LR15)
Analyse AlphaFold monomer V2.0 prediction for tRNA-modifying protein ygfz (C3LR15) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C3LR15
- Type
- protein
- Length
- 323 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7FDF8b382C6a36A8772D1A265E8e480c7DF0A9C1
- Molecule
- TRNA-modifying protein ygfz
- UniProt
- C3LR15
- Pockets
- 4 · best druggability 0.59
Structure
1 distinct chain · 22% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TRNA-modifying protein ygfz | protein | 323 | 22% helix, 36% strand | C3LR15 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 373 | 0.59 | 0.76 | 43 | empty |
| 2 | 102 | 0.34 | 0.73 | 17 | empty |
| 3 | 84 | 0.33 | 0.75 | 16 | empty |
| 4 | 68 | 0.31 | 0.75 | 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 C3LR15
- Elsewhere: UniProt C3LR15 · AlphaFold DB C3LR15
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