Research workbench
AlphaFold monomer V2.0 prediction for 2-aminoethylphosphonate-- pyruvate transaminase (C3LAM8)
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
- C3LAM8
- Type
- protein
- Length
- 365 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- 2-aminoethylphosphonate--pyruvate transaminase
- UniProt
- C3LAM8
- Pockets
- 3 · best druggability 0.50
Structure
1 distinct chain · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2-aminoethylphosphonate--pyruvate transaminase | protein | 365 | 42% helix, 18% strand | C3LAM8 |
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 | 115 | 0.50 | 0.81 | 26 | empty |
| 2 | 92 | 0.41 | 0.78 | 17 | empty |
| 3 | 91 | 0.32 | 0.73 | 22 | 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 C3LAM8
- Elsewhere: UniProt C3LAM8 · AlphaFold DB C3LAM8
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