Research workbench
AlphaFold monomer V2.0 prediction for trans-2,3-enoyl-CoA reductase- like (Q5HYJ1)
Analyse AlphaFold monomer V2.0 prediction for trans-2,3-enoyl-CoA reductase- like… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5HYJ1
- Type
- protein
- Length
- 363 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6Ed09D80e98fE15DE51C9E7a8896AbF1f2365C3e
- Molecule
- Trans-2,3-enoyl-CoA reductase-like
- UniProt
- Q5HYJ1
- Pockets
- 3 · best druggability 0.74
Structure
1 distinct chain · 56% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trans-2,3-enoyl-CoA reductase-like | protein | 363 | 56% helix, 11% strand | Q5HYJ1 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 192 | 0.74 | 0.90 | 40 | empty |
| 2 | 151 | 0.59 | 0.83 | 25 | empty |
| 3 | 329 | 0.56 | 0.75 | 32 | 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 Q5HYJ1
- Elsewhere: UniProt Q5HYJ1 · AlphaFold DB Q5HYJ1
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