1hmu: Difference between revisions

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[[Image:1hmu.png|left|200px]]


{{STRUCTURE_1hmu|  PDB=1hmu  |  SCENE=  }}
==ACTIVE SITE OF CHONDROITINASE AC LYASE REVEALED BY THE STRUCTURE OF ENZYME-OLIGOSACCHARIDE COMPLEXES AND MUTAGENESIS==
 
<StructureSection load='1hmu' size='340' side='right'caption='[[1hmu]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
===ACTIVE SITE OF CHONDROITINASE AC LYASE REVEALED BY THE STRUCTURE OF ENZYME-OLIGOSACCHARIDE COMPLEXES AND MUTAGENESIS===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1hmu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pedobacter_heparinus Pedobacter heparinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HMU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HMU FirstGlance]. <br>
{{ABSTRACT_PUBMED_11327856}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASG:2-DEOXY-2-ACETAMIDO-BETA-D-GALACTOSE-4-SULFATE'>ASG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GCD:4,5-DEHYDRO-D-GLUCURONIC+ACID'>GCD</scene>, <scene name='pdbligand=GCU:D-GLUCURONIC+ACID'>GCU</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MXY:2-O-METHYL+FUCOSE'>MXY</scene>, <scene name='pdbligand=RAM:ALPHA-L-RHAMNOSE'>RAM</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hmu OCA], [https://pdbe.org/1hmu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hmu RCSB], [https://www.ebi.ac.uk/pdbsum/1hmu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hmu ProSAT]</span></td></tr>
[[1hmu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pedobacter_heparinus Pedobacter heparinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HMU OCA].  
</table>
 
== Function ==
==Reference==
[https://www.uniprot.org/uniprot/CSLA_PEDHD CSLA_PEDHD]
<ref group="xtra">PMID:011327856</ref><references group="xtra"/>
== Evolutionary Conservation ==
[[Category: Chondroitin AC lyase]]
[[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/hm/1hmu_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/main_output.php?pdb_ID=1hmu ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pedobacter heparinus]]
[[Category: Pedobacter heparinus]]
[[Category: Boju, L.]]
[[Category: Boju L]]
[[Category: Cygler, M.]]
[[Category: Cygler M]]
[[Category: Gunay, N S.]]
[[Category: Gunay NS]]
[[Category: Huang, W.]]
[[Category: Huang W]]
[[Category: Kim, Y S.]]
[[Category: Kim YS]]
[[Category: Linhardt, R J.]]
[[Category: Linhardt RJ]]
[[Category: Matte, A.]]
[[Category: Matte A]]
[[Category: Su, H.]]
[[Category: Su H]]
[[Category: Tkalec, L.]]
[[Category: Tkalec L]]
[[Category: Yang, H O.]]
[[Category: Yang HO]]
[[Category: Active site]]
[[Category: Catalysis]]
[[Category: Lyase]]
[[Category: Protein-oligosaccharide complex]]

Latest revision as of 11:33, 27 March 2024

ACTIVE SITE OF CHONDROITINASE AC LYASE REVEALED BY THE STRUCTURE OF ENZYME-OLIGOSACCHARIDE COMPLEXES AND MUTAGENESIS

1hmu, resolution 2.00Å

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