1jmf: Difference between revisions

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[[Image:1jmf.png|left|200px]]


{{STRUCTURE_1jmf|  PDB=1jmf  |  SCENE=  }}
==CONTRIBUTIONS OF ORIENTATION AND HYDROGEN BONDING TO CATALYSIS IN ASN-229 MUTANTS OF THYMIDYLATE SYNTHASE==
 
<StructureSection load='1jmf' size='340' side='right'caption='[[1jmf]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
===CONTRIBUTIONS OF ORIENTATION AND HYDROGEN BONDING TO CATALYSIS IN ASN-229 MUTANTS OF THYMIDYLATE SYNTHASE===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1jmf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lacticaseibacillus_casei Lacticaseibacillus casei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JMF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JMF FirstGlance]. <br>
{{ABSTRACT_PUBMED_9514716}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jmf OCA], [https://pdbe.org/1jmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jmf RCSB], [https://www.ebi.ac.uk/pdbsum/1jmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jmf ProSAT]</span></td></tr>
[[1jmf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lactobacillus_casei Lactobacillus casei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JMF OCA].  
</table>
== Function ==
[https://www.uniprot.org/uniprot/TYSY_LACCA TYSY_LACCA] Provides the sole de novo source of dTMP for DNA biosynthesis.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jm/1jmf_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1jmf ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Thymidylate synthase|Thymidylate synthase]]
*[[Thymidylate synthase 3D structures|Thymidylate synthase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:009514716</ref><references group="xtra"/>
[[Category: Lacticaseibacillus casei]]
[[Category: Lactobacillus casei]]
[[Category: Large Structures]]
[[Category: Thymidylate synthase]]
[[Category: Finer-Moore J]]
[[Category: Finer-Moore, J.]]
[[Category: Stroud RM]]
[[Category: Stroud, R M.]]
[[Category: Methyltransferase]]
[[Category: Transferase]]

Latest revision as of 10:40, 7 February 2024

CONTRIBUTIONS OF ORIENTATION AND HYDROGEN BONDING TO CATALYSIS IN ASN-229 MUTANTS OF THYMIDYLATE SYNTHASECONTRIBUTIONS OF ORIENTATION AND HYDROGEN BONDING TO CATALYSIS IN ASN-229 MUTANTS OF THYMIDYLATE SYNTHASE

Structural highlights

1jmf is a 1 chain structure with sequence from Lacticaseibacillus casei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TYSY_LACCA Provides the sole de novo source of dTMP for DNA biosynthesis.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1jmf, resolution 2.50Å

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