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AlphaFold monomer V2.0 prediction for glutamate-1-semialdehyde 2,1-aminomutase (A7FM09)
Analyse AlphaFold monomer V2.0 prediction for glutamate-1-semialdehyde 2,1-aminomutase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7FM09
- Type
- protein
- Length
- 426 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x82b6765f0e89D0Ef5ceCDAEcdAE1d82fe8434df4
- Molecule
- Glutamate-1-semialdehyde 2,1-aminomutase
- UniProt
- A7FM09
- Pockets
- 4 · best druggability 0.63
Structure
1 distinct chain · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate-1-semialdehyde 2,1-aminomutase | protein | 426 | 40% helix, 18% strand | A7FM09 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 510 | 0.63 | 0.76 | 48 | empty |
| 2 | 194 | 0.51 | 0.76 | 23 | empty |
| 3 | 105 | 0.35 | 0.73 | 20 | empty |
| 4 | 62 | 0.33 | 0.76 | 16 | 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 A7FM09
- Elsewhere: UniProt A7FM09 · AlphaFold DB A7FM09
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