1z53

<table><tr><td colspan='2'>[[1z53]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z53 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Z53 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PP9:PROTOPORPHYRIN+IX'>PP9</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2cyp|2cyp]], [[1kok|1kok]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CCP1, CCP, CPO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1z53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z53 OCA], [http://pdbe.org/1z53 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z53 RCSB], [http://www.ebi.ac.uk/pdbsum/1z53 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z53 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/CCPR_YEAST CCPR_YEAST]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

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== Publication Abstract from PubMed ==

The iron-free cytochrome c peroxidase (CCP) crystal structure has been determined to 1.13 A and compared with the 1.2-A ferric-CCP structure. Quite unexpectedly, removal of the iron has no effect on porphyrin geometry and distortion, indicating that protein-porphyrin interactions and not iron coordination or formation of the axial His-Fe bond determines porphyrin conformation. However, there are changes in solvent structure in the distal pocket, which lead to changes in the distal His52 acid-base catalyst. The observed ability of His52 to move in response to small changes in solvent structure is very likely important for its role as a catalyst in assisting in the heterolytic fission of the peroxide O-O bond.

The 1.13-A structure of iron-free cytochrome c peroxidase.,Bhaskar B, Poulos TL J Biol Inorg Chem. 2005 Jun;10(4):425-30. Epub 2005 May 18. PMID:15900441<ref>PMID:15900441</ref>

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

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== References ==

<references/>

[[Category: Atcc 18824]]

[[Category: Cytochrome-c peroxidase]]

[[Category: Bhaskar, B]]

[[Category: Poulos, T L]]

[[Category: Ccp]]

[[Category: Trp cation radical]]