4otl
From Proteopedia
X-ray Crystal Structure of Serine Hydroxymethyl Transferase from Burkholderia cenocepacia bound to PLP and Glycine
Function
[B4ECY9_BURCJ] Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism (By similarity).[HAMAP-Rule:MF_00051]
About this Structure
4otl is a 4 chain structure. Full crystallographic information is available from OCA.
Categories: Glycine hydroxymethyltransferase | SSGCID, Seattle Structural Genomics Center for Infectious Disease. | National institute of allergy and infectious disease | Niaid | Seattle structural genomics center for infectious disease | Serine hydroxymethyl transferase | Ssgcid | Structural genomic | Transferase
