4p2p: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(12 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:4p2p.jpg|left|200px]]


{{Structure
==AN INDEPENDENT CRYSTALLOGRAPHIC REFINEMENT OF PORCINE PHOSPHOLIPASE A2 AT 2.4 ANGSTROMS RESOLUTION==
|PDB= 4p2p |SIZE=350|CAPTION= <scene name='initialview01'>4p2p</scene>, resolution 2.4&Aring;
<StructureSection load='4p2p' size='340' side='right'caption='[[4p2p]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
<table><tr><td colspan='2'>[[4p2p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P2P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P2P FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
|GENE=
<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>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4p2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p2p OCA], [https://pdbe.org/4p2p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p2p RCSB], [https://www.ebi.ac.uk/pdbsum/4p2p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p2p ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PA21B_PIG PA21B_PIG] PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
== 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/p2/4p2p_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=4p2p ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Porcine phospholipase A2 (Mr = 13,980), trigonal, P3(1)21, a = b = 69.4, c = 70.4 A, one molecule per asymmetric unit, lambda (Cu K alpha) = 1.54 A. Model incorporating 975 protein atoms and eight solvent molecules refined by restrained least-squares fit to a residual R = 0.21 for 6382 reflections from 5 to 2.4 A resolution.


'''AN INDEPENDENT CRYSTALLOGRAPHIC REFINEMENT OF PORCINE PHOSPHOLIPASE A2 AT 2.4 ANGSTROMS RESOLUTION'''
An independent crystallographic refinement of porcine phospholipase A2 at 2.4 A resolution.,Finzel BC, Ohlendorf DH, Weber PC, Salemme FR Acta Crystallogr B. 1991 Aug 1;47 ( Pt 4):558-9. PMID:1930837<ref>PMID:1930837</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4p2p" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Porcine phospholipase A2 (Mr = 13,980), trigonal, P3(1)21, a = b = 69.4, c = 70.4 A, one molecule per asymmetric unit, lambda (Cu K alpha) = 1.54 A. Model incorporating 975 protein atoms and eight solvent molecules refined by restrained least-squares fit to a residual R = 0.21 for 6382 reflections from 5 to 2.4 A resolution.
*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
 
== References ==
==About this Structure==
<references/>
4P2P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P2P OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
An independent crystallographic refinement of porcine phospholipase A2 at 2.4 A resolution., Finzel BC, Ohlendorf DH, Weber PC, Salemme FR, Acta Crystallogr B. 1991 Aug 1;47 ( Pt 4):558-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1930837 1930837]
[[Category: Phospholipase A(2)]]
[[Category: Single protein]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Finzel, B C.]]
[[Category: Finzel BC]]
[[Category: Ohlendorf, D H.]]
[[Category: Ohlendorf DH]]
[[Category: Salemme, F R.]]
[[Category: Salemme FR]]
[[Category: Weber, P C.]]
[[Category: Weber PC]]
[[Category: CA]]
[[Category: carboxylic ester hydrolase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:10:30 2008''

Latest revision as of 11:16, 6 November 2024

AN INDEPENDENT CRYSTALLOGRAPHIC REFINEMENT OF PORCINE PHOSPHOLIPASE A2 AT 2.4 ANGSTROMS RESOLUTION

4p2p, resolution 2.40Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA