This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3gf0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (15:39, 1 November 2023) (edit) (undo)
 
Line 3: Line 3:
<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 [https://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 [https://proteopedia.org/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" id="ligandDat"><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"><div style='overflow: auto; max-height: 3em;'>[[1ogh|1ogh]], [[2hxd|2hxd]], [[2hxb|2hxb]]</div></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'>[https://en.wikipedia.org/wiki/dCTP_deaminase_(dUMP-forming) dCTP deaminase (dUMP-forming)], with EC number [https://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'>[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>
</table>
</table>
== Function ==
== Function ==
-
[[https://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]]
Line 24: Line 23:
==See Also==
==See Also==
*[[Deaminase 3D structures|Deaminase 3D structures]]
*[[Deaminase 3D structures|Deaminase 3D structures]]
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Atcc 43067]]
 
[[Category: Large Structures]]
[[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]]
+

Current revision

Bifunctional dCTP deaminase-dUTPase mutant enzyme variant E145Q from Methanocaldococcus jannaschii in complex with pyrophosphate and magnesium

PDB ID 3gf0

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3gf0"
Personal tools