4yta

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'''Unreleased structure'''
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==BOND LENGTH ANALYSIS OF ASP, GLU AND HIS RESIDUES IN TRYPSIN AT 1.2A RESOLUTION==
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<StructureSection load='4yta' size='340' side='right' caption='[[4yta]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4yta]] 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=4YTA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YTA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3unr|3unr]]</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span></td></tr>
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<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=4yta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yta OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4yta RCSB], [http://www.ebi.ac.uk/pdbsum/4yta PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A bond-distance analysis has been undertaken to determine the protonation states of ionizable amino acids in trypsin, subtilisin and lysozyme. The diffraction resolutions were 1.2 A for trypsin (97% complete, 12% H-atom visibility at 2.5sigma), 1.26 A for subtilisin (100% complete, 11% H-atom visibility at 2.5sigma) and 0.65 A for lysozyme (PDB entry 2vb1; 98% complete, 30% H-atom visibility at 3sigma). These studies provide a wide diffraction resolution range for assessment. The bond-length e.s.d.s obtained are as small as 0.008 A and thus provide an exceptional opportunity for bond-length analyses. The results indicate that useful information can be obtained from diffraction data at around 1.2-1.3 A resolution and that minor increases in resolution can have significant effects on reducing the associated bond-length standard deviations. The protonation states in histidine residues were also considered; however, owing to the smaller differences between the protonated and deprotonated forms it is much more difficult to infer the protonation states of these residues. Not even the 0.65 A resolution lysozyme structure provided the necessary accuracy to determine the protonation states of histidine.
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The entry 4yta is ON HOLD
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Protonation-state determination in proteins using high-resolution X-ray crystallography: effects of resolution and completeness.,Fisher SJ, Blakeley MP, Cianci M, McSweeney S, Helliwell JR Acta Crystallogr D Biol Crystallogr. 2012 Jul;68(Pt 7):800-9. doi:, 10.1107/S0907444912012589. Epub 2012 Jun 15. PMID:22751665<ref>PMID:22751665</ref>
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Authors: Fisher, S.J., Helliwell, J.R., Blakeley, M.P., Cianci, M., McSweeny, S.
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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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Description: BOND LENGTH ANALYSIS OF ASP, GLU AND HIS RESIDUES IN TRYPSIN AT 1.2A RESOLUTION
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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[[Category: Fisher, S.J]]
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__TOC__
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[[Category: Blakeley, M.P]]
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</StructureSection>
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[[Category: Helliwell, J.R]]
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[[Category: Bos taurus]]
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[[Category: Mcsweeny, S]]
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[[Category: Trypsin]]
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[[Category: Blakeley, M P]]
[[Category: Cianci, M]]
[[Category: Cianci, M]]
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[[Category: Fisher, S J]]
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[[Category: Helliwell, J R]]
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[[Category: McSweeny, S]]
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[[Category: Hydrolase]]
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[[Category: Serine protease]]

Revision as of 15:49, 27 May 2015

BOND LENGTH ANALYSIS OF ASP, GLU AND HIS RESIDUES IN TRYPSIN AT 1.2A RESOLUTION

4yta, resolution 1.20Å

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