1mkt

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{{Seed}}
 
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[[Image:1mkt.png|left|200px]]
 
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==CARBOXYLIC ESTER HYDROLASE, 1.72 ANGSTROM TRIGONAL FORM OF THE BOVINE RECOMBINANT PLA2 ENZYME==
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The line below this paragraph, containing "STRUCTURE_1mkt", creates the "Structure Box" on the page.
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<StructureSection load='1mkt' size='340' side='right'caption='[[1mkt]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1mkt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MKT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MKT FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.72&#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=CA:CALCIUM+ION'>CA</scene></td></tr>
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{{STRUCTURE_1mkt| PDB=1mkt | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mkt OCA], [https://pdbe.org/1mkt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mkt RCSB], [https://www.ebi.ac.uk/pdbsum/1mkt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mkt ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PA21B_BOVIN PA21B_BOVIN] PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mk/1mkt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1mkt ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The trigonal crystal structure of the recombinant bovine pancreatic phospholipase A2 has been re-refined at a slightly higher resolution (1.72 A). The crystals are trigonal, space group P3121, unit-cell parameters a = b = 46.78 and c = 102.89 A and are isomorphous to the previous structure. The structure was refined to a final crystallographic R value of 19.5% (Rfree = 28.4%) using 10 531 reflections. A total of 106 solvent molecules were included in the refinement compared with the earlier refinement which contains only 85 water molecules and 8 925 reflections at 1.8 A resolution. The root-mean-square deviation from the ideal bond lengths and bond angles is considerably better in the present refinement. The active site is extended ( approximately 14 A) from Ala1 to the calcium. The three catalytic residues (Asp99, His48 and the catalytic water) are connected by the conserved structural water and the N-terminal Ala1 on one side, and by the calcium through an equatorial water on the other. The water molecules play a role in the activity of the enzyme PLA2. The Ala1 end of the extended active site performs the activation of the phospholid membranes while the opposite end performs the hydrolysis of the monomeric phospholids.
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===CARBOXYLIC ESTER HYDROLASE, 1.72 ANGSTROM TRIGONAL FORM OF THE BOVINE RECOMBINANT PLA2 ENZYME===
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1.72 A resolution refinement of the trigonal form of bovine pancreatic phospholipase A2.,Sekar K, Sekharudu C, Tsai MD, Sundaralingam M Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):342-6. PMID:9761901<ref>PMID:9761901</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1mkt" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_9761901}}, adds the Publication Abstract to the page
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*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 9761901 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_9761901}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1MKT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MKT OCA].
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==Reference==
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1.72 A resolution refinement of the trigonal form of bovine pancreatic phospholipase A2., Sekar K, Sekharudu C, Tsai MD, Sundaralingam M, Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):342-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9761901 9761901]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Sundaralingam, M.]]
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[[Category: Sundaralingam M]]
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[[Category: Carboxylic ester hydrolase]]
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[[Category: Enzyme]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 00:12:59 2008''
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Current revision

CARBOXYLIC ESTER HYDROLASE, 1.72 ANGSTROM TRIGONAL FORM OF THE BOVINE RECOMBINANT PLA2 ENZYME

PDB ID 1mkt

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