3bg9

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(New page: 200px<br /><applet load="3bg9" size="350" color="white" frame="true" align="right" spinBox="true" caption="3bg9, resolution 3.000&Aring;" /> '''Crystal Structure o...)
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[[Image:3bg9.jpg|left|200px]]<br /><applet load="3bg9" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="3bg9, resolution 3.000&Aring;" />
 
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'''Crystal Structure of Human Pyruvate Carboxylase (missing the biotin carboxylase domain at the N-terminus) F1077A Mutant'''<br />
 
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==About this Structure==
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==Crystal Structure of Human Pyruvate Carboxylase (missing the biotin carboxylase domain at the N-terminus) F1077A Mutant==
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3BG9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pyruvate_carboxylase Pyruvate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.1 6.4.1.1] Known structural/functional Sites: <scene name='pdbsite=AC1:Mn+Binding+Site+For+Residue+A+2001'>AC1</scene>, <scene name='pdbsite=AC2:Mn+Binding+Site+For+Residue+B+2001'>AC2</scene>, <scene name='pdbsite=AC3:Mn+Binding+Site+For+Residue+C+2001'>AC3</scene> and <scene name='pdbsite=AC4:Mn+Binding+Site+For+Residue+D+2001'>AC4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BG9 OCA].
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<StructureSection load='3bg9' size='340' side='right'caption='[[3bg9]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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[[Category: Homo sapiens]]
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== Structural highlights ==
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[[Category: Pyruvate carboxylase]]
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<table><tr><td colspan='2'>[[3bg9]] 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=3BG9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BG9 FirstGlance]. <br>
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[[Category: Single protein]]
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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]] 3&#8491;</td></tr>
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[[Category: Tong, L.]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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[[Category: Xiang, S.]]
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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=3bg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bg9 OCA], [https://pdbe.org/3bg9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bg9 RCSB], [https://www.ebi.ac.uk/pdbsum/3bg9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bg9 ProSAT]</span></td></tr>
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[[Category: MN]]
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</table>
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[[Category: atp-binding]]
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== Disease ==
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[[Category: biotin]]
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[https://www.uniprot.org/uniprot/PYC_HUMAN PYC_HUMAN] Defects in PC are the cause of pyruvate carboxylase deficiency (PC deficiency) [MIM:[https://omim.org/entry/266150 266150]. PC deficiency leads to lactic acidosis, mental retardation and death. It occurs in three forms: mild or type A, severe neonatal or type B, and a very mild lacticacidemia.
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[[Category: disease mutation]]
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== Function ==
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[[Category: gluconeogenesis]]
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[https://www.uniprot.org/uniprot/PYC_HUMAN PYC_HUMAN] Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate.
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[[Category: ligase]]
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== Evolutionary Conservation ==
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[[Category: lipid synthesis]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: manganese]]
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Check<jmol>
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[[Category: mitochondrion]]
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<jmolCheckbox>
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[[Category: multifunctional enzyme]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bg/3bg9_consurf.spt"</scriptWhenChecked>
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[[Category: nucleotide-binding]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: phosphoprotein]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: tim barrel]]
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</jmolCheckbox>
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[[Category: transit peptide]]
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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=3bg9 ConSurf].
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<div style="clear:both"></div>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 27 07:59:41 2008''
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==See Also==
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*[[Pyruvate carboxylase 3D structures|Pyruvate carboxylase 3D structures]]
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Tong L]]
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[[Category: Xiang S]]

Current revision

Crystal Structure of Human Pyruvate Carboxylase (missing the biotin carboxylase domain at the N-terminus) F1077A Mutant

PDB ID 3bg9

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