5h4j: Difference between revisions

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'''Unreleased structure'''


The entry 5h4j is ON HOLD  until Nov 01 2018
==Crystal structure of Human dUTPase in complex with N-[(1R)-1-[3-(Cyclopentyloxy)-phenyl]-ethyl]-3-[(3,4-dihydro-2,4-dioxo-1(2H)-pyrimidinyl)methoxy]-1-propanesulfonamide==
 
<StructureSection load='5h4j' size='340' side='right' caption='[[5h4j]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
Authors: Chong, K.T., Miyahara, S., Miyakoshi, H., Fukuoka, M.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5h4j]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H4J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H4J FirstGlance]. <br>
Description: Crystal structure of Human dUTPase in complex with N-[(1R)-1-[3-(Cyclopentyloxy)-phenyl]-ethyl]-3-[(3,4-dihydro-2,4-dioxo-1(2H)-pyrimidinyl)methoxy]-1-propanesulfonamide
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=FKM:N-[(1R)-1-[3-(Cyclopentyloxy)-phenyl]-ethyl]-3-[(3,4-dihydro-2,4-dioxo-1(2H)-pyrimidinyl)methoxy]-1-propanesulfonamide'>FKM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dUTP_diphosphatase dUTP diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.23 3.6.1.23] </span></td></tr>
[[Category: Miyakoshi, H]]
<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=5h4j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h4j OCA], [http://pdbe.org/5h4j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h4j RCSB], [http://www.ebi.ac.uk/pdbsum/5h4j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h4j ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/DUT_HUMAN DUT_HUMAN]] This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.<ref>PMID:8805593</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: DUTP diphosphatase]]
[[Category: Chong, K T]]
[[Category: Fukuoka, M]]
[[Category: Fukuoka, M]]
[[Category: Miyahara, S]]
[[Category: Miyahara, S]]
[[Category: Chong, K.T]]
[[Category: Miyakoshi, H]]
[[Category: Hydrolase]]
[[Category: Hydrolase inhibitor]]
[[Category: Hydrolase-hydrolase inhibitor complex]]

Revision as of 09:24, 1 November 2017

Crystal structure of Human dUTPase in complex with N-[(1R)-1-[3-(Cyclopentyloxy)-phenyl]-ethyl]-3-[(3,4-dihydro-2,4-dioxo-1(2H)-pyrimidinyl)methoxy]-1-propanesulfonamideCrystal structure of Human dUTPase in complex with N-[(1R)-1-[3-(Cyclopentyloxy)-phenyl]-ethyl]-3-[(3,4-dihydro-2,4-dioxo-1(2H)-pyrimidinyl)methoxy]-1-propanesulfonamide

Structural highlights

5h4j is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
Activity:dUTP diphosphatase, with EC number 3.6.1.23
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DUT_HUMAN] This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.[1]

References

  1. ↑ Mol CD, Harris JM, McIntosh EM, Tainer JA. Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits. Structure. 1996 Sep 15;4(9):1077-92. PMID:8805593

5h4j, resolution 1.80Å

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