4x4k | pdb_00004x4k

Structure of laccase from Botrytis aclada with full copper content

spinqualitylabelsall models 4x4k, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4x4k is a 1 chain structure with sequence from Botrytis aclada. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BMA, CU, MAN, NAG, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function H8ZRU2_9HELO Publication Abstract from PubMed Laccases belong to the class of multicopper oxidases catalyzing the oxidation of phenols accompanied by the reduction of molecular oxygen to water without the formation of hydrogen peroxide. The activity of laccases depends on the number of Cu atoms per enzyme molecule. The structure of type 2 copper-depleted laccase from Botrytis aclada has been solved previously. With the aim of obtaining the structure of the native form of the enzyme, crystals of the depleted laccase were soaked in Cu(+)- and Cu(2+)-containing solutions. Copper ions were found to be incorporated into the active site only when Cu(+) was used. A comparative analysis of the native and depleted forms of the enzymes was performed. Incorporation of copper ions into crystals of T2 copper-depleted laccase from Botrytis aclada.,Osipov EM, Polyakov KM, Tikhonova TV, Kittl R, Dorovatovskii PV, Shleev SV, Popov VO, Ludwig R Acta Crystallogr F Struct Biol Commun. 2015 Dec 1;71(Pt 12):1465-9. doi:, 10.1107/S2053230X1502052X. Epub 2015 Nov 18. PMID:26625287 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Laccase 3D structures

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