1f4j

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[[Image:1f4j.jpg|left|200px]]
 
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{{Structure
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==STRUCTURE OF TETRAGONAL CRYSTALS OF HUMAN ERYTHROCYTE CATALASE==
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|PDB= 1f4j |SIZE=350|CAPTION= <scene name='initialview01'>1f4j</scene>, resolution 2.40&Aring;
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<StructureSection load='1f4j' size='340' side='right'caption='[[1f4j]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene>
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<table><tr><td colspan='2'>[[1f4j]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F4J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F4J FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Catalase Catalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6]
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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]] 2.4&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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}}
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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=1f4j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f4j OCA], [https://pdbe.org/1f4j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f4j RCSB], [https://www.ebi.ac.uk/pdbsum/1f4j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f4j ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/CATA_HUMAN CATA_HUMAN] Defects in CAT are the cause of acatalasemia (ACATLAS) [MIM:[https://omim.org/entry/614097 614097]. A metabolic disorder characterized by absence of catalase activity in red cells and is often associated with ulcerating oral lesions.<ref>PMID:2308162</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/CATA_HUMAN CATA_HUMAN] Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells.<ref>PMID:7882369</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f4/1f4j_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f4j ConSurf].
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<div style="clear:both"></div>
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'''STRUCTURE OF TETRAGONAL CRYSTALS OF HUMAN ERYTHROCYTE CATALASE'''
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==See Also==
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*[[Catalase 3D structures|Catalase 3D structures]]
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== References ==
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==Overview==
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<references/>
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The structure of catalase from human erythrocytes (HEC) was determined in tetragonal crystals of space group I4(1) by molecular-replacement methods, using the orthorhombic crystal structure as a search model. It was then refined in a unit cell of dimensions a = b = 203.6 and c = 144.6 A, yielding R and R(free) of 0.196 and 0.244, respectively, for all data at 2.4 A resolution. A major difference of the HEC structure in the tetragonal crystal compared with the orthorhombic structure was the omission of a 20-residue N-terminal segment corresponding to the first exon of the human catalase gene. The overall structures were otherwise identical in both crystal forms. The NADPH-binding sites were empty in all four subunits and bound water molecules were observed at the active sites. The structure of the C-terminal segment, which corresponds to the last exon, remained undetermined. The tetragonal crystals showed a pseudo-4(1)22 symmetry in molecular packing. Two similar types of lattice contact interfaces between the HEC tetramers were observed; they were related by the pseudo-dyad axes.
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__TOC__
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</StructureSection>
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==Disease==
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Known disease associated with this structure: Acatalasemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=115500 115500]]
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==About this Structure==
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1F4J is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F4J OCA].
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==Reference==
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Structure of tetragonal crystals of human erythrocyte catalase., Safo MK, Musayev FN, Wu SH, Abraham DJ, Ko TP, Acta Crystallogr D Biol Crystallogr. 2001 Jan;57(Pt 1):1-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11134921 11134921]
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[[Category: Catalase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Abraham, D J.]]
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[[Category: Abraham DJ]]
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[[Category: Ko, T P.]]
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[[Category: Ko TP]]
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[[Category: Musayev, F N.]]
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[[Category: Musayev FN]]
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[[Category: Safo, M K.]]
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[[Category: Safo MK]]
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[[Category: Wu, S H.]]
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[[Category: Wu SH]]
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[[Category: HEM]]
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[[Category: heme protein]]
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[[Category: no bound nadph]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:04:29 2008''
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Current revision

STRUCTURE OF TETRAGONAL CRYSTALS OF HUMAN ERYTHROCYTE CATALASE

PDB ID 1f4j

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