Research workbench
AlphaFold monomer V2.0 prediction for tryptophan synthase beta chain (A1VY69)
Analyse AlphaFold monomer V2.0 prediction for tryptophan synthase beta chain (A1VY69) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1VY69
- Type
- protein
- Length
- 392 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5881B09f2D8e743400698633641fc1cD2Ed2BE6F
- Molecule
- Tryptophan synthase beta chain
- UniProt
- A1VY69
- Pockets
- 4 · best druggability 0.80
Structure
1 distinct chain · 47% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tryptophan synthase beta chain | protein | 392 | 47% helix, 20% strand | A1VY69 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 147 | 0.80 | 0.97 | 35 | empty |
| 2 | 74 | 0.42 | 0.80 | 15 | empty |
| 3 | 98 | 0.39 | 0.75 | 25 | empty |
| 4 | 56 | 0.38 | 0.80 | 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 A1VY69
- Elsewhere: UniProt A1VY69 · AlphaFold DB A1VY69
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