1mnp

<table><tr><td colspan='2'>[[1mnp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Phanerochaete_chrysosporium Phanerochaete chrysosporium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MNP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MNP FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7] </span></td></tr>

[[https://www.uniprot.org/uniprot/PEM1_PHACH PEM1_PHACH]] Catalyzes the oxidation of Mn(2+) to Mn(3+). The latter, acting as a diffusible redox mediator, is capable of oxidizing a variety of lignin compounds.

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== Publication Abstract from PubMed ==

Manganese peroxidase from the white rot basidiomycete Phanerochaete chrysosporium has been crystallized in a form suitable for high-resolution X-ray structure determination. Crystals were grown from solutions containing 30% polyethylene glycol 8000, ammonium sulfate and cacodylate buffer at pH 6.5, using macroseeding techniques. A complete data set has been obtained to 2.06 A resolution. The data can be indexed in space group P1 with a = 45.96 A, b = 53.77 A, c = 84.87 A, alpha = 97.01 degrees, beta = 105.72 degrees and gamma = 90.1 degrees, with two peroxidase molecules per asymmetric unit, or in space group C2 with a = 163.23 A, b = 45.97 A, c = 53.72 A and beta = 97.16 degrees, with only one molecule in the assymetric unit. Lignin peroxidase, which shares about 57% sequence identity with manganese peroxidase, was used as a probe for molecular replacement. Unique rotation and translation solutions have been obtained in space groups P1 and C2. The structure has been partially refined in space group C2 to R = 0.22 for data between 10 and 2.06 A.

Preliminary crystallographic analysis of manganese peroxidase from Phanerochaete chrysosporium.,Sundaramoorthy M, Kishi K, Gold MH, Poulos TL J Mol Biol. 1994 May 20;238(5):845-8. PMID:8182752<ref>PMID:8182752</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Peroxidase]]

[[Category: Phanerochaete chrysosporium]]

[[Category: Poulos, T L]]

[[Category: Sundaramoorthy, M]]

[[Category: Heme peroxidase]]