Research workbench
AlphaFold monomer V2.0 prediction for N-fatty-acyl-amino acid SYNTHASE/HYDROLASE PM20D1.1 (Q32LT9)
Analyse AlphaFold monomer V2.0 prediction for N-fatty-acyl-amino acid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q32LT9
- Type
- protein
- Length
- 515 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x93bBF2fe56740B1134A77aBB4c1B98d1631fF1Be
- Molecule
- N-fatty-acyl-amino acid SYNTHASE/HYDROLASE PM20D1.1
- UniProt
- Q32LT9
- Pockets
- 3 · best druggability 0.73
Structure
1 distinct chain · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-fatty-acyl-amino acid SYNTHASE/HYDROLASE PM20D1.1 | protein | 515 | 39% helix, 23% strand | Q32LT9 |
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 | 645 | 0.73 | 0.79 | 56 | empty |
| 2 | 50 | 0.45 | 0.84 | 14 | empty |
| 3 | 136 | 0.42 | 0.75 | 20 | 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 Q32LT9
- Elsewhere: UniProt Q32LT9 · AlphaFold DB Q32LT9
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