1ahp

OLIGOSACCHARIDE SUBSTRATE BINDING IN ESCHERICHIA COLI MALTODEXTRIN PHSPHORYLASEOLIGOSACCHARIDE SUBSTRATE BINDING IN ESCHERICHIA COLI MALTODEXTRIN PHSPHORYLASE

Structural highlights 1ahp is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3Å Ligands: , , , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PHSM_ECOLI 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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

spinqualitylabelsall models 1ahp, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image