1ua7: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ua7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UA7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UA7 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1ua7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UA7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UA7 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=G6D:6-DEOXY-ALPHA-D-GLUCOSE'>G6D</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GLD:4,6-DIDEOXYGLUCOSE'>GLD</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=G6D:6-DEOXY-ALPHA-D-GLUCOSE'>G6D</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GLD:4,6-DIDEOXYGLUCOSE'>GLD</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACI:6-AMINO-4-HYDROXYMETHYL-CYCLOHEX-4-ENE-1,2,3-TRIOL'>ACI</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACI:6-AMINO-4-HYDROXYMETHYL-CYCLOHEX-4-ENE-1,2,3-TRIOL'>ACI</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bag|1bag]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bag|1bag]]</td></tr> | ||
<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ua7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ua7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ua7 RCSB], [http://www.ebi.ac.uk/pdbsum/1ua7 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=1ua7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ua7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ua7 RCSB], [http://www.ebi.ac.uk/pdbsum/1ua7 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 30: | Line 30: | ||
==See Also== | ==See Also== | ||
*[[Amylase|Amylase]] | *[[Amylase|Amylase]] | ||
*[[User:Gabriel Pons/Sandbox 2|User:Gabriel Pons/Sandbox 2]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 36: | Line 37: | ||
[[Category: Alpha-amylase]] | [[Category: Alpha-amylase]] | ||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Fujimoto, Z | [[Category: Fujimoto, Z]] | ||
[[Category: Kagawa, M | [[Category: Kagawa, M]] | ||
[[Category: Mizuno, H | [[Category: Mizuno, H]] | ||
[[Category: Momma, M | [[Category: Momma, M]] | ||
[[Category: Takase, K | [[Category: Takase, K]] | ||
[[Category: Acarbose]] | [[Category: Acarbose]] | ||
[[Category: Beta-alpha-barrel]] | [[Category: Beta-alpha-barrel]] | ||
[[Category: Greek-key motif]] | [[Category: Greek-key motif]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 16:14, 6 January 2015
Crystal Structure Analysis of Alpha-Amylase from Bacillus Subtilis complexed with AcarboseCrystal Structure Analysis of Alpha-Amylase from Bacillus Subtilis complexed with Acarbose
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of Bacillus subtilis alpha-amylase, in complex with the pseudotetrasaccharide inhibitor acarbose, revealed an hexasaccharide in the active site as a result of transglycosylation. After comparison with the known structure of the catalytic-site mutant complexed with the native substrate maltopentaose, it is suggested that the present structure represents a mimic intermediate in the initial stage of the catalytic process. Crystal structure of Bacillus subtilis alpha-amylase in complex with acarbose.,Kagawa M, Fujimoto Z, Momma M, Takase K, Mizuno H J Bacteriol. 2003 Dec;185(23):6981-4. PMID:14617662[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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