2wr8 | pdb_00002wr8

Structure of Pyrococcus horikoshii SAM hydroxide adenosyltransferase in complex with SAH

spinqualitylabelsall models 2wr8, resolution 1.77Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wr8 is a 1 chain structure with sequence from Pyrococcus horikoshii OT3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.77Å Ligands: SAH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RSAMH_PYRHO Catalyzes the hydrolysis of S-adenosyl-L-methionine (SAM) into adenosine and L-methionine (PubMed:18551689). Is likely stereoselective, specifically hydrolyzing (R)-S-adenosyl-L-methionine ((R)-SAM), the inactive form of the ubiquitous cofactor SAM, and not the active form of SAM, (S)-S-adenosyl-L-methionine (By similarity). Probaly plays a role in preventing accumulation of (R)-S-adenosyl-L-methionine in cells; maintenance of (S)-S-denosyl-L-methionine homochirality is important for cellular health given that the (R)-form is largely inactive as a methyl donor and can function as an inhibitor of methyltransferases (By similarity). Is unable to mediate a fluorination or chlorination reaction with SAM (PubMed:18551689).[UniProtKB:A4X4S2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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