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4c51

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<StructureSection load='4c51' size='340' side='right'caption='[[4c51]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
<StructureSection load='4c51' size='340' side='right'caption='[[4c51]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4c51]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C51 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C51 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4c51]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C51 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C51 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c50|4c50]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Catalase_peroxidase Catalase peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.21 1.11.1.21] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4c51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c51 OCA], [https://pdbe.org/4c51 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c51 RCSB], [https://www.ebi.ac.uk/pdbsum/4c51 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c51 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4c51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c51 OCA], [http://pdbe.org/4c51 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c51 RCSB], [http://www.ebi.ac.uk/pdbsum/4c51 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c51 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/KATG_MYCTU KATG_MYCTU]] Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Displays also NADH oxidase, isoniazid (INH) lyase and isonicotinoyl-NAD synthase activity. May play a role in the intracellular survival of mycobacteria. May be involved in DNA repair. Partly complements recA-deficient E.coli cells exposed to UV radiation, mitomycin C or hydrogen peroxide. Increases resistance to mitomycin C in E.coli cells deficient for either uvrA, uvrB or uvrC.<ref>PMID:10463167</ref>
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[https://www.uniprot.org/uniprot/KATG_MYCTU KATG_MYCTU] Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Displays also NADH oxidase, isoniazid (INH) lyase and isonicotinoyl-NAD synthase activity. May play a role in the intracellular survival of mycobacteria. May be involved in DNA repair. Partly complements recA-deficient E.coli cells exposed to UV radiation, mitomycin C or hydrogen peroxide. Increases resistance to mitomycin C in E.coli cells deficient for either uvrA, uvrB or uvrC.<ref>PMID:10463167</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
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*[[Catalase|Catalase]]
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*[[Catalase 3D structures|Catalase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Catalase peroxidase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Myctu]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Andersson, K K]]
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[[Category: Andersson KK]]
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[[Category: Hersleth, H P]]
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[[Category: Hersleth H-P]]
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[[Category: Magliozzo, R S]]
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[[Category: Magliozzo RS]]
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[[Category: Zhao, X]]
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[[Category: Zhao X]]
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[[Category: Oxidoreductase]]
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Current revision

Crystal Structure of the Catalase-Peroxidase (KatG) R418L mutant from Mycobacterium Tuberculosis

PDB ID 4c51

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