4hpj | pdb_00004hpj
From Proteopedia
Crystal structure of Tryptophan Synthase at 1.45 A resolution in complex with 2-aminophenol quinonoid in the beta site and the F9 inhibitor in the alpha site
Function
[TRPA_SALTY] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. [TRPB_SALTY] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
About this Structure
4hpj is a 2 chain structure. Full crystallographic information is available from OCA.
Reference
- Niks D, Hilario E, Dierkers A, Ngo H, Borchardt D, Neubauer TJ, Fan L, Mueller LJ, Dunn MF. Allostery and substrate channeling in the tryptophan synthase bienzyme complex: evidence for two subunit conformations and four quaternary states. Biochemistry. 2013 Sep 17;52(37):6396-411. doi: 10.1021/bi400795e. Epub 2013 Sep , 6. PMID:23952479 doi:https://dx.doi.org/10.1021/bi400795e
