2cag | pdb_00002cag

CATALASE COMPOUND II

spinqualitylabelsall models 2cag, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2cag is a 1 chain structure with sequence from Proteus mirabilis. The September 2004 RCSB PDB Molecule of the Month feature on Catalase by David S. Goodsell is 10.2210/rcsb_pdb/mom_2004_9. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HEM NonStd Res: OMT Activity: Catalase, with EC number 1.11.1.6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CATA_PROMI] Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Various enzymes use semi-stable ferryl intermediates and free radicals during their catalytic cycle, amongst them haem catalases. Structures for two transient intermediates (compounds I and II) of the NADPH-dependent catalase from Proteus mirabilis (PMC) have been determined by time-resolved X-ray crystallography and single crystal microspectrophotometry. The results show the formation and transformation of the ferryl group in the haem, and the unexpected binding of an anion during this reaction at a site distant from the haem. Ferryl intermediates of catalase captured by time-resolved Weissenberg crystallography and UV-VIS spectroscopy.,Gouet P, Jouve HM, Williams PA, Andersson I, Andreoletti P, Nussaume L, Hajdu J Nat Struct Biol. 1996 Nov;3(11):951-6. PMID:8901874 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Catalase Catalase 2CAG bcce2014

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