Research workbench
AlphaFold monomer V2.0 prediction for probable tRNA pseudouridine synthase B (A1RTL7)
Analyse AlphaFold monomer V2.0 prediction for probable tRNA pseudouridine synthase B… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1RTL7
- Type
- protein
- Length
- 328 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa4785222Bbe47502ED0a362Ddab993F3F3B268aC
- Molecule
- Probable tRNA pseudouridine synthase B
- UniProt
- A1RTL7
- Pockets
- 3 · best druggability 0.60
Structure
1 distinct chain · 29% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable tRNA pseudouridine synthase B | protein | 328 | 29% helix, 32% strand | A1RTL7 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 250 | 0.60 | 0.80 | 34 | empty |
| 2 | 83 | 0.45 | 0.81 | 16 | empty |
| 3 | 64 | 0.27 | 0.73 | 13 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 A1RTL7
- Elsewhere: UniProt A1RTL7 · AlphaFold DB A1RTL7
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