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[[Image:1qqw.png|left|200px]]


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==CRYSTAL STRUCTURE OF HUMAN ERYTHROCYTE CATALASE==
The line below this paragraph, containing "STRUCTURE_1qqw", creates the "Structure Box" on the page.
<StructureSection load='1qqw' size='340' side='right'caption='[[1qqw]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1qqw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The September 2004 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Catalase''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2004_9 10.2210/rcsb_pdb/mom_2004_9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QQW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QQW FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
{{STRUCTURE_1qqw| PDB=1qqw |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qqw OCA], [https://pdbe.org/1qqw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qqw RCSB], [https://www.ebi.ac.uk/pdbsum/1qqw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qqw ProSAT]</span></td></tr>
</table>
== Disease ==
[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>
== Function ==
[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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qq/1qqw_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1qqw ConSurf].
<div style="clear:both"></div>


'''CRYSTAL STRUCTURE OF HUMAN ERYTHROCYTE CATALASE'''
==See Also==
 
*[[Catalase|Catalase]]
 
*[[Catalase 3D structures|Catalase 3D structures]]
{{ABSTRACT_10666617}}
== References ==
 
<references/>
==About this Structure==
__TOC__
1QQW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1QQW with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb57_1.html Catalase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QQW OCA].
</StructureSection>
[[Category: Catalase]]
[[Category: Catalase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Abraham, D J.]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Ko, T P.]]
[[Category: Abraham DJ]]
[[Category: Musayev, F N.]]
[[Category: Ko TP]]
[[Category: Safo, M K.]]
[[Category: Musayev FN]]
[[Category: Wang, C.]]
[[Category: Safo MK]]
[[Category: Wu, S H.]]
[[Category: Wang C]]
[[Category: Heme protein]]
[[Category: Wu SH]]
[[Category: Lattice contact]]
[[Category: No nadp]]
[[Category: Water]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 17:52:42 2008''

Latest revision as of 11:16, 14 February 2024

CRYSTAL STRUCTURE OF HUMAN ERYTHROCYTE CATALASECRYSTAL STRUCTURE OF HUMAN ERYTHROCYTE CATALASE

Structural highlights

1qqw is a 4 chain structure with sequence from Homo sapiens. The September 2004 RCSB PDB Molecule of the Month feature on Catalase by David S. Goodsell is 10.2210/rcsb_pdb/mom_2004_9. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.75Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

CATA_HUMAN Defects in CAT are the cause of acatalasemia (ACATLAS) [MIM:614097. A metabolic disorder characterized by absence of catalase activity in red cells and is often associated with ulcerating oral lesions.[1]

Function

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.[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Wen JK, Osumi T, Hashimoto T, Ogata M. Molecular analysis of human acatalasemia. Identification of a splicing mutation. J Mol Biol. 1990 Jan 20;211(2):383-93. PMID:2308162 doi:http://dx.doi.org/10.1016/0022-2836(90)90359-T
  2. ↑ Takeuchi A, Miyamoto T, Yamaji K, Masuho Y, Hayashi M, Hayashi H, Onozaki K. A human erythrocyte-derived growth-promoting factor with a wide target cell spectrum: identification as catalase. Cancer Res. 1995 Apr 1;55(7):1586-9. PMID:7882369

1qqw, resolution 2.75Å

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