2o2e: Difference between revisions

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==Mycobacterium tuberculosis tryptophan synthase beta subunit dimer (apoform)==
==Mycobacterium tuberculosis tryptophan synthase beta subunit dimer (apoform)==
<StructureSection load='2o2e' size='340' side='right' caption='[[2o2e]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='2o2e' size='340' side='right' caption='[[2o2e]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">trpB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">trpB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20] </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=2o2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o2e OCA], [http://pdbe.org/2o2e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o2e RCSB], [http://www.ebi.ac.uk/pdbsum/2o2e PDBsum]</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=2o2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o2e OCA], [http://pdbe.org/2o2e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o2e RCSB], [http://www.ebi.ac.uk/pdbsum/2o2e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2o2e ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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].
</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=2o2e ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
==See Also==
*[[Tryptophan synthase|Tryptophan synthase]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 11:50, 18 October 2017

Mycobacterium tuberculosis tryptophan synthase beta subunit dimer (apoform)Mycobacterium tuberculosis tryptophan synthase beta subunit dimer (apoform)

Structural highlights

2o2e is a 2 chain structure with sequence from "bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:trpB ("Bacillus tuberculosis" (Zopf 1883) Klein 1884)
Activity:Tryptophan synthase, with EC number 4.2.1.20
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TRPB_MYCTU] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine (By similarity).

Evolutionary Conservation

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

2o2e, resolution 2.20Å

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OCA