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3dhp
From Proteopedia
(Difference between revisions)
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==Probing the role of aromatic residues at the secondary saccharide binding sites of human salivary alpha-amylase in substrate hydrolysis and bacterial binding== | ==Probing the role of aromatic residues at the secondary saccharide binding sites of human salivary alpha-amylase in substrate hydrolysis and bacterial binding== | ||
<StructureSection load='3dhp' size='340' side='right' caption='[[3dhp]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='3dhp' size='340' side='right' caption='[[3dhp]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3dhp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DHP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DHP FirstGlance]. <br> | <table><tr><td colspan='2'>[[3dhp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DHP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DHP FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=HMC:5-HYDROXYMETHYL-CHONDURITOL'>HMC | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGL:4,6-DIDEOXY-4-AMINO-ALPHA-D-GLUCOSE'>AGL</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=HMC:5-HYDROXYMETHYL-CHONDURITOL'>HMC</scene></td></tr> |
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1smd|1smd]], [[1mfv|1mfv]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1smd|1smd]], [[1mfv|1mfv]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] </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=3dhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dhp OCA], [http://pdbe.org/3dhp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3dhp RCSB], [http://www.ebi.ac.uk/pdbsum/3dhp 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=3dhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dhp OCA], [http://pdbe.org/3dhp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3dhp RCSB], [http://www.ebi.ac.uk/pdbsum/3dhp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3dhp ProSAT]</span></td></tr> |
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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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=3dhp 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=3dhp ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
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| - | ==See Also== | ||
| - | *[[Amylase|Amylase]] | ||
| - | *[[User:Gabriel Pons/Sandbox 2|User:Gabriel Pons/Sandbox 2]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
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[[Category: Sait, H M]] | [[Category: Sait, H M]] | ||
[[Category: Amylase acarbose aromatic residues mutagenesis]] | [[Category: Amylase acarbose aromatic residues mutagenesis]] | ||
| + | [[Category: Calcium]] | ||
[[Category: Carbohydrate metabolism]] | [[Category: Carbohydrate metabolism]] | ||
[[Category: Chloride]] | [[Category: Chloride]] | ||
Revision as of 08:50, 25 October 2017
Probing the role of aromatic residues at the secondary saccharide binding sites of human salivary alpha-amylase in substrate hydrolysis and bacterial binding
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