1qqw: Difference between revisions

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


{{STRUCTURE_1qqw|  PDB=1qqw  |  SCENE=  }}
==CRYSTAL STRUCTURE OF HUMAN ERYTHROCYTE CATALASE==
 
<StructureSection load='1qqw' size='340' side='right'caption='[[1qqw]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
===CRYSTAL STRUCTURE OF HUMAN ERYTHROCYTE CATALASE===
== Structural highlights ==
 
<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>
{{ABSTRACT_PUBMED_10666617}}
</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>
 
<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>
==About this Structure==
<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>
[[1qqw]] is a 4 chain structure of [[Catalase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The September 2004 RCSB PDB [http://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 [http://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].  
</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>


==See Also==
==See Also==
*[[Catalase|Catalase]]
*[[Catalase|Catalase]]
 
*[[Catalase 3D structures|Catalase 3D structures]]
==Reference==
== References ==
<ref group="xtra">PMID:010666617</ref><references group="xtra"/>
<references/>
__TOC__
</StructureSection>
[[Category: Catalase]]
[[Category: Catalase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Abraham, D J.]]
[[Category: Abraham DJ]]
[[Category: Ko, T P.]]
[[Category: Ko TP]]
[[Category: Musayev, F N.]]
[[Category: Musayev FN]]
[[Category: Safo, M K.]]
[[Category: Safo MK]]
[[Category: Wang, C.]]
[[Category: Wang C]]
[[Category: Wu, S H.]]
[[Category: Wu SH]]
[[Category: Heme protein]]
[[Category: Lattice contact]]
[[Category: No nadp]]
[[Category: Oxidoreductase]]
[[Category: Water]]

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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