Research workbench
AlphaFold monomer V2.0 prediction for glutamate-1-semialdehyde 2,1-aminomutase (Q478V1)
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
- Q478V1
- Type
- protein
- Length
- 427 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x37980899ba05b13cE955B2984E29ee9e423A1753
- Molecule
- Glutamate-1-semialdehyde 2,1-aminomutase
- UniProt
- Q478V1
- Pockets
- 3 · best druggability 0.63
Structure
1 distinct chain · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate-1-semialdehyde 2,1-aminomutase | protein | 427 | 42% helix, 17% strand | Q478V1 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 508 | 0.63 | 0.76 | 50 | empty |
| 2 | 282 | 0.58 | 0.78 | 40 | empty |
| 3 | 136 | 0.42 | 0.75 | 28 | 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 Q478V1
- Elsewhere: UniProt Q478V1 · AlphaFold DB Q478V1
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