3a1f: Difference between revisions

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<StructureSection load='3a1f' size='340' side='right'caption='[[3a1f]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3a1f' size='340' side='right'caption='[[3a1f]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3a1f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A1F OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3A1F FirstGlance]. <br>
<table><tr><td colspan='2'>[[3a1f]] is a 1 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=3A1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A1F FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
</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&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3a1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a1f OCA], [http://pdbe.org/3a1f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a1f RCSB], [http://www.ebi.ac.uk/pdbsum/3a1f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a1f ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3a1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a1f OCA], [https://pdbe.org/3a1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a1f RCSB], [https://www.ebi.ac.uk/pdbsum/3a1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a1f ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/CY24B_HUMAN CY24B_HUMAN]] Defects in CYBB are a cause of granulomatous disease,chronic, X-linked (CGD) [MIM:[http://omim.org/entry/306400 306400]]. A disorder characterized by the inability of neutrophils and phagocytes to kill microbes that they have ingested. Patients suffer from life-threatening bacterial/fungal infections.<ref>PMID:12139950</ref> <ref>PMID:2556453</ref> <ref>PMID:1710153</ref> <ref>PMID:8101486</ref> <ref>PMID:7927345</ref> <ref>PMID:8182143</ref> <ref>PMID:8916969</ref> <ref>PMID:9111587</ref> <ref>PMID:9585602</ref> <ref>PMID:9856476</ref> <ref>PMID:9794433</ref> <ref>PMID:9667376</ref> <ref>PMID:10089913</ref> <ref>PMID:9888386</ref> <ref>PMID:10914676</ref> <ref>PMID:11462241</ref> <ref>PMID:11997083</ref> <ref>PMID:15338276</ref> <ref>PMID:18773283</ref> <ref>PMID:22125116</ref>  Defects in CYBB are a cause of mycobacteriosis atypical X-linked type 2 (AMCBX2) [MIM:[http://omim.org/entry/300645 300645]]. A rare condition characterized by predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine and environmental non-tuberculous mycobacteria, and by the more virulent Mycobacterium tuberculosis. Other microorganisms rarely cause severe clinical disease in individuals with susceptibility to mycobacterial infections.<ref>PMID:21278736</ref>
[https://www.uniprot.org/uniprot/CY24B_HUMAN CY24B_HUMAN] Defects in CYBB are a cause of granulomatous disease,chronic, X-linked (CGD) [MIM:[https://omim.org/entry/306400 306400]. A disorder characterized by the inability of neutrophils and phagocytes to kill microbes that they have ingested. Patients suffer from life-threatening bacterial/fungal infections.<ref>PMID:12139950</ref> <ref>PMID:2556453</ref> <ref>PMID:1710153</ref> <ref>PMID:8101486</ref> <ref>PMID:7927345</ref> <ref>PMID:8182143</ref> <ref>PMID:8916969</ref> <ref>PMID:9111587</ref> <ref>PMID:9585602</ref> <ref>PMID:9856476</ref> <ref>PMID:9794433</ref> <ref>PMID:9667376</ref> <ref>PMID:10089913</ref> <ref>PMID:9888386</ref> <ref>PMID:10914676</ref> <ref>PMID:11462241</ref> <ref>PMID:11997083</ref> <ref>PMID:15338276</ref> <ref>PMID:18773283</ref> <ref>PMID:22125116</ref>  Defects in CYBB are a cause of mycobacteriosis atypical X-linked type 2 (AMCBX2) [MIM:[https://omim.org/entry/300645 300645]. A rare condition characterized by predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine and environmental non-tuberculous mycobacteria, and by the more virulent Mycobacterium tuberculosis. Other microorganisms rarely cause severe clinical disease in individuals with susceptibility to mycobacterial infections.<ref>PMID:21278736</ref>  
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CY24B_HUMAN CY24B_HUMAN]] Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes. It participates in the regulation of cellular pH and is blocked by zinc.  
[https://www.uniprot.org/uniprot/CY24B_HUMAN CY24B_HUMAN] Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes. It participates in the regulation of cellular pH and is blocked by zinc.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=3a1f ConSurf].
</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=3a1f ConSurf].
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==See Also==
*[[NADPH oxidase 3D structures|NADPH oxidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Honbou, K]]
[[Category: Honbou K]]
[[Category: Nadph binding domain]]
[[Category: Oxidoreductase]]