Research workbench
AlphaFold monomer V2.0 prediction for pkhd-type hydroxylase P9301_13621 (A3PE10)
Analyse AlphaFold monomer V2.0 prediction for pkhd-type hydroxylase P9301_13621 (A3PE10) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A3PE10
- Type
- protein
- Length
- 222 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- Pkhd-type hydroxylase P9301_13621
- UniProt
- A3PE10
- Pockets
- 1 · best druggability 0.69
Structure
1 distinct chain · 39% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pkhd-type hydroxylase P9301_13621 | protein | 222 | 39% helix, 33% strand | A3PE10 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 172 | 0.69 | 0.88 | 36 | 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 A3PE10
- Elsewhere: UniProt A3PE10 · AlphaFold DB A3PE10
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