2c4m

STARCH PHOSPHORYLASE: STRUCTURAL STUDIES EXPLAIN OXYANION-DEPENDENT KINETIC STABILITY AND REGULATORY CONTROL.STARCH PHOSPHORYLASE: STRUCTURAL STUDIES EXPLAIN OXYANION-DEPENDENT KINETIC STABILITY AND REGULATORY CONTROL.

Structural highlights 2c4m is a 4 chain structure with sequence from Atcc 15991. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , , , Activity: Phosphorylase, with EC number 2.4.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [Q8KQ56_9CORY] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.[RuleBase:RU000587] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also Glycogen Phosphorylase

spinqualitylabelsall models 2c4m, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image