Research workbench
AlphaFold monomer V2.0 prediction for indole-3-glycerol phosphate synthase (A5VXL5)
Analyse AlphaFold monomer V2.0 prediction for indole-3-glycerol phosphate synthase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5VXL5
- Type
- protein
- Length
- 277 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x71112d4fF7ebb3b617963c05f052289e073082FD
- Molecule
- Indole-3-glycerol phosphate synthase
- UniProt
- A5VXL5
- Pockets
- 3 · best druggability 0.81
Structure
1 distinct chain · 49% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Indole-3-glycerol phosphate synthase | protein | 277 | 49% helix, 17% strand | A5VXL5 |
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 | 201 | 0.81 | 0.94 | 33 | empty |
| 2 | 54 | 0.45 | 0.84 | 19 | empty |
| 3 | 120 | 0.40 | 0.75 | 18 | 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 A5VXL5
- Elsewhere: UniProt A5VXL5 · AlphaFold DB A5VXL5
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