1f4j: Difference between revisions

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{{Seed}}
[[Image:1f4j.png|left|200px]]


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==STRUCTURE OF TETRAGONAL CRYSTALS OF HUMAN ERYTHROCYTE CATALASE==
The line below this paragraph, containing "STRUCTURE_1f4j", creates the "Structure Box" on the page.
<StructureSection load='1f4j' size='340' side='right'caption='[[1f4j]], [[Resolution|resolution]] 2.40&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'>[[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>
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]] 2.4&#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_1f4j| PDB=1f4j |  SCENE= }}
<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>
</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/f4/1f4j_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=1f4j ConSurf].
<div style="clear:both"></div>


===STRUCTURE OF TETRAGONAL CRYSTALS OF HUMAN ERYTHROCYTE CATALASE===
==See Also==
 
*[[Catalase 3D structures|Catalase 3D structures]]
 
== References ==
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{{ABSTRACT_PUBMED_11134921}}
 
==About this Structure==
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].
 
==Reference==
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]
[[Category: Catalase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[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: Wu, S H.]]
[[Category: Wu SH]]
[[Category: Heme protein]]
[[Category: No bound nadph]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 02:40:38 2008''

Latest revision as of 10:10, 7 February 2024

STRUCTURE OF TETRAGONAL CRYSTALS OF HUMAN ERYTHROCYTE CATALASESTRUCTURE OF TETRAGONAL CRYSTALS OF HUMAN ERYTHROCYTE CATALASE

Structural highlights

1f4j is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
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

1f4j, resolution 2.40Å

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