1h3j

STRUCTURE OF RECOMBINANT COPRINUS CINEREUS PEROXIDASE DETERMINED TO 2.0 A

spinqualitylabelsall models 1h3j, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1h3j is a 2 chain structure with sequence from Coprinopsis cinerea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: BMA, CA, HEM, MG, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PER_COPCI 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 The structure of the peroxidase from Coprinus cinereus (CiP) has been determined in three different space groups and crystalline environments. Two of these are of the recombinant glycosylated form (rCiP), which crystallized in space groups P2(1)2(1)2(1) and C2. The third crystal form was obtained from a variant of CiP in which the glycosylation sites have been removed (rCiPON). It crystallizes in space group P2(1) with beta approximately 90 degrees; the structure was determined from room-temperature data and low-temperature data obtained from twinned crystals. Two independent molecules of CiP related by non-crystallographic symmetry are contained in the three crystal forms. The packing in the two structures of the glycosylated form of rCiP is closely related, but differs from the packing in the unglycosylated rCiPON. A database search based on small-molecule porphinato iron (III) complexes has been performed and related to observations of the spin states and coordination numbers of the iron ion. The room-temperature structures of CiP and one structure of the almost identical peroxidase from Arthromyces ramosus (ARP) have been used to identify 66 conserved water molecules and to assign a structural role to most of them. Impact of the physical and chemical environment on the molecular structure of Coprinus cinereus peroxidase.,Houborg K, Harris P, Petersen J, Rowland P, Poulsen JC, Schneider P, Vind J, Larsen S Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):989-96. Epub 2003, May 23. PMID:12777760 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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