4bp2
From Proteopedia
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| - | [[ | + | ==CRYSTALLOGRAPHIC REFINEMENT OF BOVINE PRO-PHOSPHOLIPASE A2 AT 1.6 ANGSTROMS RESOLUTION== |
| + | <StructureSection load='4bp2' size='340' side='right' caption='[[4bp2]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4bp2]] is a 1 chain structure with 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=4BP2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BP2 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bp2|2bp2]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
| + | <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=4bp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bp2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bp2 RCSB], [http://www.ebi.ac.uk/pdbsum/4bp2 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/bp/4bp2_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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bovine pro-phospholipase A2 (Mr = 14,520), trigonal, P3(1)21, a = b = 46.5, c = 102.0 A, one molecule per asymmetric unit, lambda (Cu K alpha) = 1.54 A. The model incorporating 895 protein atoms, two molecules of 2-methyl-2,4-pentanediol, and 60 solvent water molecules, was refined by restrained least squares to a residual R = 0.194 for 14,667 reflections from 5 to 1.6 A resolution. | ||
| - | + | Crystallographic refinement of bovine pro-phospholipase A2 at 1.6 A resolution.,Finzel BC, Weber PC, Ohlendorf DH, Salemme FR Acta Crystallogr B. 1991 Oct 1;47 ( Pt 5):814-6. PMID:1793547<ref>PMID:1793547</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Phospholipase A2|Phospholipase A2]] | *[[Phospholipase A2|Phospholipase A2]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
| - | [[Category: Finzel, B C | + | [[Category: Finzel, B C]] |
| - | [[Category: Ohlendorf, D H | + | [[Category: Ohlendorf, D H]] |
| - | [[Category: Salemme, F R | + | [[Category: Salemme, F R]] |
| - | [[Category: Weber, P C | + | [[Category: Weber, P C]] |
[[Category: Carboxylic ester hydrolase zymogen]] | [[Category: Carboxylic ester hydrolase zymogen]] | ||
Revision as of 15:02, 9 December 2014
CRYSTALLOGRAPHIC REFINEMENT OF BOVINE PRO-PHOSPHOLIPASE A2 AT 1.6 ANGSTROMS RESOLUTION
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