6ogn | pdb_00006ogn

Crystal structure of mouse protein arginine methyltransferase 7 in complex with SGC8158 chemical probe

spinqualitylabelsall models 6ogn, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ogn is a 1 chain structure. This structure supersedes the now removed PDB entry 6npg. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MJ7, UNX, ZN Activity: Type III protein arginine methyltransferase, with EC number 2.1.1.321 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ANM7_MOUSE] Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo (By similarity).

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