Research workbench
AlphaFold monomer V2.0 prediction for tryptophanase (Q9CL27)
Analyse AlphaFold monomer V2.0 prediction for tryptophanase (Q9CL27) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9CL27
- Type
- protein
- Length
- 471 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x977800eEe8528a9947f5111a1A455f29D20a6478
- Molecule
- Tryptophanase
- UniProt
- Q9CL27
- Pockets
- 6 · best druggability 0.66
Structure
1 distinct chain · 46% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tryptophanase | protein | 471 | 46% helix, 14% strand | Q9CL27 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 184 | 0.66 | 0.85 | 40 | empty |
| 2 | 77 | 0.63 | 0.91 | 30 | empty |
| 3 | 356 | 0.61 | 0.77 | 40 | empty |
| 4 | 73 | 0.41 | 0.80 | 16 | empty |
| 5 | 72 | 0.38 | 0.78 | 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 Q9CL27
- Elsewhere: UniProt Q9CL27 · AlphaFold DB Q9CL27
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