1com

THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS: STRUCTURE DETERMINATION OF CHORISMATE MUTASE AND ITS COMPLEXES WITH A TRANSITION STATE ANALOG AND PREPHENATE, AND IMPLICATIONS ON THE MECHANISM OF ENZYMATIC REACTIONTHE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS: STRUCTURE DETERMINATION OF CHORISMATE MUTASE AND ITS COMPLEXES WITH A TRANSITION STATE ANALOG AND PREPHENATE, AND IMPLICATIONS ON THE MECHANISM OF ENZYMATIC REACTION

Structural highlights 1com is a 12 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AROH_BACSU Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also 3D structures of chorismate mutase

spinqualitylabelsall models 1com, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image