2via

CRYSTAL STRUCTURE OF S172ABSSHMT L-SERINE EXTERNAL ALDIMINECRYSTAL STRUCTURE OF S172ABSSHMT L-SERINE EXTERNAL ALDIMINE

Structural highlights 2via is a 1 chain structure with sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , , , Related: 2vgu, 1yjy, 2vi9, 1yjs, 1kl2, 2vi8, 1kl1, 1kkp, 2vgs, 1yjz, 2vgt, 2vgv, 1kkj, 2vgw, 2vib Activity: Glycine hydroxymethyltransferase, with EC number 2.1.2.1 Resources: FirstGlance, OCA, RCSB, PDBsum Function [Q7SIB6_BACST] 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] Interconversion of serine and glycine (By similarity).[RuleBase:RU000585] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also Serine hydroxymethyltransferase

spinqualitylabelsall models 2via, resolution 1.67Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image