Research workbench
AlphaFold monomer V2.0 prediction for tRNA hydroxylation protein P (P76403)
Analyse AlphaFold monomer V2.0 prediction for tRNA hydroxylation protein P (P76403) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P76403
- Type
- protein
- Length
- 453 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA5374D84395c453698039b71Cc29bC29eAD7b8BD
- Molecule
- TRNA hydroxylation protein P
- UniProt
- P76403
- Pockets
- 4 · best druggability 0.75
Structure
1 distinct chain · 27% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TRNA hydroxylation protein P | protein | 453 | 27% helix, 27% strand | P76403 |
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 | 756 | 0.75 | 0.80 | 71 | empty |
| 2 | 138 | 0.43 | 0.75 | 20 | empty |
| 3 | 95 | 0.43 | 0.78 | 28 | empty |
| 4 | 109 | 0.40 | 0.76 | 15 | 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 P76403
- Elsewhere: UniProt P76403 · AlphaFold DB P76403
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