Research workbench
AlphaFold monomer V2.0 prediction for tryptophan synthase beta chain 1 (P50909)
Analyse AlphaFold monomer V2.0 prediction for tryptophan synthase beta chain 1 (P50909) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P50909
- Type
- protein
- Length
- 389 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5BeA89782341f98147F2D811B063F91F0aE7D7bF
- Molecule
- Tryptophan synthase beta chain 1
- UniProt
- P50909
- Pockets
- 3 · best druggability 0.78
Structure
1 distinct chain · 49% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tryptophan synthase beta chain 1 | protein | 389 | 49% helix, 20% strand | P50909 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 133 | 0.78 | 0.96 | 35 | empty |
| 2 | 155 | 0.56 | 0.82 | 28 | empty |
| 3 | 51 | 0.38 | 0.81 | 19 | empty |
Compared structures
- 8EGZ · Engineered tyrosine synthase (TmTyrS1) derived from T. maritima TrpB with Ser bound as… · an experimental structure of the same protein · chain A against B, TM-score 0.98
- 8EH1 · Engineered tyrosine synthase (TmTyrS1) derived from T. maritima TrpB with Ser bound as… · an experimental structure of the same protein · chain A against B, TM-score 0.98
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 P50909
- Elsewhere: UniProt P50909 · AlphaFold DB P50909
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