1xnb: Difference between revisions

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[[Image:1xnb.jpg|left|200px]]


{{Structure
==HIGH-RESOLUTION STRUCTURES OF XYLANASES FROM B. CIRCULANS AND T. HARZIANUM IDENTIFY A NEW FOLDING PATTERN AND IMPLICATIONS FOR THE ATOMIC BASIS OF THE CATALYSIS==
|PDB= 1xnb |SIZE=350|CAPTION= <scene name='initialview01'>1xnb</scene>, resolution 1.49&Aring;
<StructureSection load='1xnb' size='340' side='right'caption='[[1xnb]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
<table><tr><td colspan='2'>[[1xnb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Niallia_circulans Niallia circulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XNB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XNB FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.49&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xnb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xnb OCA], [https://pdbe.org/1xnb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xnb RCSB], [https://www.ebi.ac.uk/pdbsum/1xnb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xnb ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xnb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xnb OCA], [http://www.ebi.ac.uk/pdbsum/1xnb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xnb RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/XYNA_NIACI XYNA_NIACI]
 
== Evolutionary Conservation ==
'''HIGH-RESOLUTION STRUCTURES OF XYLANASES FROM B. CIRCULANS AND T. HARZIANUM IDENTIFY A NEW FOLDING PATTERN AND IMPLICATIONS FOR THE ATOMIC BASIS OF THE CATALYSIS'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==About this Structure==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xn/1xnb_consurf.spt"</scriptWhenChecked>
1XNB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_circulans Bacillus circulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XNB OCA].  
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: Bacillus circulans]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: Endo-1,4-beta-xylanase]]
  </jmolCheckbox>
[[Category: Single protein]]
</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=1xnb ConSurf].
[[Category: Campbell, R L.]]
<div style="clear:both"></div>
[[Category: glycosidase]]
__TOC__
 
</StructureSection>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:52:01 2008''
[[Category: Large Structures]]
[[Category: Niallia circulans]]
[[Category: Campbell RL]]

Latest revision as of 08:51, 14 February 2024

HIGH-RESOLUTION STRUCTURES OF XYLANASES FROM B. CIRCULANS AND T. HARZIANUM IDENTIFY A NEW FOLDING PATTERN AND IMPLICATIONS FOR THE ATOMIC BASIS OF THE CATALYSIS

1xnb, resolution 1.49Å

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