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==Bifunctional dCTP deaminase-dUTPase mutant enzyme variant E145Q from Methanocaldococcus jannaschii in complex with pyrophosphate and magnesium==
==Bifunctional dCTP deaminase-dUTPase mutant enzyme variant E145Q from Methanocaldococcus jannaschii in complex with pyrophosphate and magnesium==
<StructureSection load='3gf0' size='340' side='right' caption='[[3gf0]], [[Resolution|resolution]] 2.62&Aring;' scene=''>
<StructureSection load='3gf0' size='340' side='right'caption='[[3gf0]], [[Resolution|resolution]] 2.62&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3gf0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2hxe 2hxe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GF0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GF0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3gf0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2hxe 2hxe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GF0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</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]] 2.62&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ogh|1ogh]], [[2hxd|2hxd]], [[2hxb|2hxb]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dCTP_deaminase_(dUMP-forming) dCTP deaminase (dUMP-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.30 3.5.4.30] </span></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=3gf0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gf0 OCA], [https://pdbe.org/3gf0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gf0 RCSB], [https://www.ebi.ac.uk/pdbsum/3gf0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gf0 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3gf0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gf0 OCA], [http://pdbe.org/3gf0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gf0 RCSB], [http://www.ebi.ac.uk/pdbsum/3gf0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3gf0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/DCD_METJA DCD_METJA]] Catalyzes two consecutive reactions to form dUMP using dCTP as substrate.[HAMAP-Rule:MF_00146]
[https://www.uniprot.org/uniprot/DCDB_METJA DCDB_METJA] Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate. It also acts as a dUTP diphosphatase with a lower affinity for dUTP than for dCTP.<ref>PMID:12538648</ref> <ref>PMID:12670946</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gf/3gf0_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gf/3gf0_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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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=3gf0 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=3gf0 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
==See Also==
*[[Deaminase 3D structures|Deaminase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 43067]]
[[Category: Large Structures]]
[[Category: Harris, P]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Helt, S S]]
[[Category: Harris P]]
[[Category: Johansson, E]]
[[Category: Helt SS]]
[[Category: Siggaard, J H.B]]
[[Category: Johansson E]]
[[Category: Vognsen, T]]
[[Category: Siggaard JHB]]
[[Category: Willemoes, M]]
[[Category: Vognsen T]]
[[Category: Bifunctional hydrolase]]
[[Category: Willemoes M]]
[[Category: Dctp deaminase-dutpase]]
[[Category: Hydrolase]]
[[Category: Magnesium]]
[[Category: Nucleotide metabolism]]