Research workbench
AlphaFold monomer V2.0 prediction for tryptophan synthase beta chain (A7H523)
Analyse AlphaFold monomer V2.0 prediction for tryptophan synthase beta chain (A7H523) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7H523
- Type
- protein
- Length
- 392 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
- Molecule
- Tryptophan synthase beta chain
- UniProt
- A7H523
- Pockets
- 4 · best druggability 0.81
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 | A7H523 |
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 | 162 | 0.81 | 0.97 | 36 | empty |
| 2 | 95 | 0.56 | 0.86 | 35 | empty |
| 3 | 80 | 0.41 | 0.78 | 14 | empty |
| 4 | 77 | 0.35 | 0.75 | 17 | 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 A7H523
- Elsewhere: UniProt A7H523 · AlphaFold DB A7H523
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