1ex3: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ex3]] 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=1EX3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EX3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ex3]] 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=1EX3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EX3 FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1] </span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</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=1ex3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ex3 OCA], [https://pdbe.org/1ex3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ex3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ex3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ex3 ProSAT]</span></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=1ex3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ex3 OCA], [https://pdbe.org/1ex3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ex3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ex3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ex3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CTRA_BOVIN CTRA_BOVIN]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1ex3 ConSurf].
</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=1ex3 ConSurf].
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<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
Protein crystals are usually obtained by an empirical approach based on extensive screening to identify suitable crystallization conditions. In contrast, we have used a systematic predictive procedure to produce data-quality crystals of bovine chymotrypsinogen A and used them to obtain a refined X-ray structure to 3 A resolution. Measurements of the osmotic second virial coefficient of chymotrypsinogen solutions were used to identify suitable solvent conditions, following which crystals were grown for approximately 30 hours by ultracentrifugal crystallization, without the use of any precipitants. Existing structures of chymotrypsinogen were obtained in solutions including 10-30 % ethanol, whereas simple buffered NaCl solutions were used here. The protein crystallized in the tetragonal space group P4(1)2(1)2, with one molecule per asymmetric unit. The quality of the refined map was very high throughout, with the main-chain atoms of all but four residues clearly defined and with nearly all side-chains also defined. Although only minor differences are seen compared to the structures previously reported, they indicate the possibility of structural changes due to the crystallization conditions used in those studies. Our results show that more systematic crystallization of proteins is possible, and that the procedure can expand the range of conditions under which crystals can be grown successfully and can make new crystal forms available.
Protein crystallization by design: chymotrypsinogen without precipitants.,Pjura PE, Lenhoff AM, Leonard SA, Gittis AG J Mol Biol. 2000 Jul 7;300(2):235-9. PMID:10873462<ref>PMID:10873462</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ex3" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Chymotrypsin 3D structures|Chymotrypsin 3D structures]]
*[[Chymotrypsin 3D structures|Chymotrypsin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Chymotrypsin]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Gittis, A G]]
[[Category: Gittis AG]]
[[Category: Lenhoff, A M]]
[[Category: Lenhoff AM]]
[[Category: Leonard, S A]]
[[Category: Leonard SA]]
[[Category: Pjura, P E]]
[[Category: Pjura PE]]
[[Category: Hydrolase]]

Revision as of 13:07, 20 March 2024

CRYSTAL STRUCTURE OF BOVINE CHYMOTRYPSINOGEN A (TETRAGONAL)CRYSTAL STRUCTURE OF BOVINE CHYMOTRYPSINOGEN A (TETRAGONAL)

Structural highlights

1ex3 is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CTRA_BOVIN

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1ex3, resolution 3.00Å

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OCA
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