4otl

X-ray Crystal Structure of Serine Hydroxymethyl Transferase from Burkholderia cenocepacia bound to PLP and Glycine

spinqualitylabelsall models 4otl, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4otl is a 4 chain structure with sequence from Burkholderia cenocepacia J2315. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: EDO, GLY, PLP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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] See Also Serine hydroxymethyltransferase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA