Research workbench
AlphaFold monomer V2.0 prediction for pkhd-type hydroxylase PPUT_0892 (A5VYU4)
Analyse AlphaFold monomer V2.0 prediction for pkhd-type hydroxylase PPUT_0892 (A5VYU4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5VYU4
- Type
- protein
- Length
- 226 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7FDF8b382C6a36A8772D1A265E8e480c7DF0A9C1
- Molecule
- Pkhd-type hydroxylase PPUT_0892
- UniProt
- A5VYU4
- Pockets
- 3 · best druggability 0.73
Structure
1 distinct chain · 35% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pkhd-type hydroxylase PPUT_0892 | protein | 226 | 35% helix, 30% strand | A5VYU4 |
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 | 69 | 0.73 | 0.98 | 28 | empty |
| 2 | 52 | 0.34 | 0.78 | 16 | empty |
| 3 | 50 | 0.26 | 0.73 | 10 | 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 A5VYU4
- Elsewhere: UniProt A5VYU4 · AlphaFold DB A5VYU4
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