Research workbench
AlphaFold monomer V2.0 prediction for 2-aminoethylphosphonate-- pyruvate transaminase (A2S233)
Analyse AlphaFold monomer V2.0 prediction for 2-aminoethylphosphonate-- pyruvate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2S233
- Type
- protein
- Length
- 369 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xea9f5858064346e9f9d471d9b68B63FAeCE0379C
- Molecule
- 2-aminoethylphosphonate--pyruvate transaminase
- UniProt
- A2S233
- Pockets
- 2 · best druggability 0.45
Structure
1 distinct chain · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2-aminoethylphosphonate--pyruvate transaminase | protein | 369 | 41% helix, 18% strand | A2S233 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 116 | 0.45 | 0.78 | 17 | empty |
| 2 | 83 | 0.40 | 0.78 | 23 | 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 A2S233
- Elsewhere: UniProt A2S233 · AlphaFold DB A2S233
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