2r59: Difference between revisions

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{{Seed}}
[[Image:2r59.jpg|left|200px]]


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==Leukotriene A4 hydrolase complexed with inhibitor RB3041==
The line below this paragraph, containing "STRUCTURE_2r59", creates the "Structure Box" on the page.
<StructureSection load='2r59' size='340' side='right'caption='[[2r59]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2r59]] is a 1 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=2R59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R59 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.89&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=PH0:N-{(2S)-3-[(R)-[(1R)-1-AMINO-2-PHENYLETHYL](HYDROXY)PHOSPHORYL]-2-BENZYLPROPANOYL}-L-PHENYLALANINE'>PH0</scene>, <scene name='pdbligand=YB:YTTERBIUM+(III)+ION'>YB</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
{{STRUCTURE_2r59| PDB=2r59 |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2r59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r59 OCA], [https://pdbe.org/2r59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r59 RCSB], [https://www.ebi.ac.uk/pdbsum/2r59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r59 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LKHA4_HUMAN LKHA4_HUMAN] Epoxide hydrolase that catalyzes the final step in the biosynthesis of the proinflammatory mediator leukotriene B4. Has also aminopeptidase activity.<ref>PMID:1897988</ref> <ref>PMID:1975494</ref> <ref>PMID:2244921</ref> <ref>PMID:12207002</ref> <ref>PMID:11917124</ref> <ref>PMID:15078870</ref> <ref>PMID:18804029</ref>
== 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/r5/2r59_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=2r59 ConSurf].
<div style="clear:both"></div>


===Leukotriene A4 hydrolase complexed with inhibitor RB3041===
==See Also==
 
*[[Leukotriene A4 Hydrolase|Leukotriene A4 Hydrolase]]
 
== References ==
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(as it appears on PubMed at http://www.pubmed.gov), where 17357161 is the PubMed ID number.
</StructureSection>
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{{ABSTRACT_PUBMED_17357161}}
 
==About this Structure==
2R59 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R59 OCA].
 
==Reference==
Assay for rapid analysis of the tri-peptidase activity of LTA4 hydrolase., Tholander F, Haeggstrom JZ, Proteins. 2007 Jun 1;67(4):1113-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17357161 17357161]
 
Leukotriene A4 hydrolase: identification of a common carboxylate recognition site for the epoxide hydrolase and aminopeptidase substrates., Rudberg PC, Tholander F, Andberg M, Thunnissen MM, Haeggstrom JZ, J Biol Chem. 2004 Jun 25;279(26):27376-82. Epub 2004 Apr 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15078870 15078870]
 
Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms., Rudberg PC, Tholander F, Thunnissen MM, Haeggstrom JZ, J Biol Chem. 2002 Jan 11;277(2):1398-404. Epub 2001 Oct 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11675384 11675384]
 
Leukotriene A4 hydrolase: selective abrogation of leukotriene B4 formation by mutation of aspartic acid 375., Rudberg PC, Tholander F, Thunnissen MM, Samuelsson B, Haeggstrom JZ, Proc Natl Acad Sci U S A. 2002 Apr 2;99(7):4215-20. Epub 2002 Mar 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11917124 11917124]
 
Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation., Thunnissen MM, Nordlund P, Haeggstrom JZ, Nat Struct Biol. 2001 Feb;8(2):131-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11175901 11175901]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Fournie-Zaluski, M C.]]
[[Category: Fournie-Zaluski MC]]
[[Category: Haeggstrom, J Z.]]
[[Category: Haeggstrom JZ]]
[[Category: Muroya, A.]]
[[Category: Muroya A]]
[[Category: Roques, B P.]]
[[Category: Roques BP]]
[[Category: Tholander, F.]]
[[Category: Tholander F]]
[[Category: Thunnissen, M.]]
[[Category: Thunnissen M]]
[[Category: Alternative splicing]]
[[Category: Analogue peptide]]
[[Category: Cytoplasm]]
[[Category: Hydrolase]]
[[Category: Hydrolysis]]
[[Category: Leukotriene biosynthesis]]
[[Category: Metal-binding]]
[[Category: Metalloprotease]]
[[Category: Multifunctional enzyme]]
[[Category: Protease]]
[[Category: Transition state]]
[[Category: Zinc]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 13 14:22:21 2008''

Latest revision as of 09:19, 21 February 2024

Leukotriene A4 hydrolase complexed with inhibitor RB3041

2r59, resolution 1.89Å

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