Research workbench
AlphaFold monomer V2.0 prediction for type I acyl-CoA thioesterase mpah' (A0A0B5LB55)
Analyse AlphaFold monomer V2.0 prediction for type I acyl-CoA thioesterase mpah'… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0A0B5LB55
- Type
- protein
- Length
- 433 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4Ef77Afb5a3D9F41c95Be3227D1CC986CCb61835
- Molecule
- Type I acyl-CoA thioesterase mpah'
- Pockets
- 3 · best druggability 0.74
Structure
1 distinct chain · 34% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Type I acyl-CoA thioesterase mpah' | protein | 433 | 34% helix, 17% strand | — |
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 | 439 | 0.74 | 0.84 | 53 | empty |
| 2 | 122 | 0.44 | 0.77 | 15 | empty |
| 3 | 61 | 0.32 | 0.76 | 18 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
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