CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
|   | 3 | Alpha Beta | 
|   | 3.20 | Alpha-Beta Barrel | 
|   | 3.20.20 | TIM Barrel | 
|   | 3.20.20.70 | Aldolase class I | 
Domain Context
CATH Clusters
| Superfamily | Aldolase class I | 
| Functional Family | Tryptophan synthase alpha chain | 
Enzyme Information
| 4.2.1.20 | Tryptophan synthase. based on mapping to UniProt P9WFY1 L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O. -!- The alpha-subunit catalyzes the conversion of 1-C-(indol-3- yl)glycerol 3-phosphate to indole and D-glyceraldehyde 3-phosphate (this reaction was listed formerly as EC 4.1.2.8). -!- The indole migrates to the beta-subunit where, in the presence of pyridoxal 5'-phosphate, it is combined with L-serine to form L-tryptophan. -!- In some organisms this enzyme is part of a multifunctional protein that also includes one or more of the enzymes EC 2.4.2.18, EC 4.1.1.48, EC 4.1.3.27 and EC 5.3.1.24. -!- In thermophilic organisms, where the high temperature enhances diffusion and causes the loss of indole, a protein similar to the beta subunit can be found (EC 4.2.1.122). -!- That enzyme cannot combine with the alpha unit of EC 4.2.1.20 to form a complex. | 
UniProtKB Entries (1)
| P9WFX9 | TRPB_MYCTU Mycobacterium tuberculosis H37Rv Tryptophan synthase beta chain | 
PDB Structure
| PDB | 5TCI | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | |
| Primary Citation | A small-molecule allosteric inhibitor of Mycobacterium tuberculosis tryptophan synthase. Nat. Chem. Biol. | 
