Research workbench
AlphaFold monomer V2.0 prediction for tryptophan synthase alpha chain (C3LLL5)
Analyse AlphaFold monomer V2.0 prediction for tryptophan synthase alpha chain (C3LLL5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C3LLL5
- Type
- protein
- Length
- 268 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xcb1EC5B5B6ffa5F727AeFD9fa20a78E85ca3141c
- Molecule
- Tryptophan synthase alpha chain
- UniProt
- C3LLL5
- Pockets
- 2 · best druggability 0.61
Structure
1 distinct chain · 50% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tryptophan synthase alpha chain | protein | 268 | 50% helix, 15% strand | C3LLL5 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 157 | 0.61 | 0.84 | 37 | empty |
| 2 | 56 | 0.29 | 0.75 | 13 | empty |
Compared structures
- 3NAV · Crystal structure of an alpha subunit of tryptophan synthase from Vibrio cholerae O1… · an experimental structure of the same protein · chain A against A, TM-score 0.94
- 3NAV · Crystal structure of an alpha subunit of tryptophan synthase from vibrio cholerae O1… · an experimental structure of the same protein · chain A against A, TM-score 0.94
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 C3LLL5
- Elsewhere: UniProt C3LLL5 · AlphaFold DB C3LLL5
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