Research workbench
AlphaFold monomer V2.0 prediction for L-proline cis-4-hydroxylase (Q92LF6)
Analyse AlphaFold monomer V2.0 prediction for L-proline cis-4-hydroxylase (Q92LF6) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q92LF6
- Type
- protein
- Length
- 280 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0EA189b2343A464f560b44103f6A3396Da1dA8a9
- Molecule
- L-proline cis-4-hydroxylase
- UniProt
- Q92LF6
- Pockets
- 3 · best druggability 0.75
Structure
1 distinct chain · 30% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-proline cis-4-hydroxylase | protein | 280 | 30% helix, 26% strand | Q92LF6 |
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 | 164 | 0.75 | 0.92 | 38 | empty |
| 2 | 87 | 0.36 | 0.75 | 18 | empty |
| 3 | 66 | 0.32 | 0.75 | 16 | 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 Q92LF6
- Elsewhere: UniProt Q92LF6 · AlphaFold DB Q92LF6
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