3ait: Difference between revisions
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<StructureSection load='3ait' size='340' side='right'caption='[[3ait]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | <StructureSection load='3ait' size='340' side='right'caption='[[3ait]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ait]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3ait]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/As_4.1460 As 4.1460]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AIT FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ait FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ait OCA], [https://pdbe.org/3ait PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ait RCSB], [https://www.ebi.ac.uk/pdbsum/3ait PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ait ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/IAA_STRTE IAA_STRTE]] Inhibits mammalian alpha-amylases specifically but has no action on plant and microbial alpha-amylases. Forms a tight stoichiometric 1:1 complex with alpha-amylase. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 17:54, 29 December 2021
RESTRAINED ENERGY REFINEMENT WITH TWO DIFFERENT ALGORITHMS AND FORCE FIELDS OF THE STRUCTURE OF THE ALPHA-AMYLASE INHIBITOR TENDAMISTAT DETERMINED BY NMR IN SOLUTIONRESTRAINED ENERGY REFINEMENT WITH TWO DIFFERENT ALGORITHMS AND FORCE FIELDS OF THE STRUCTURE OF THE ALPHA-AMYLASE INHIBITOR TENDAMISTAT DETERMINED BY NMR IN SOLUTION
Structural highlights
Function[IAA_STRTE] Inhibits mammalian alpha-amylases specifically but has no action on plant and microbial alpha-amylases. Forms a tight stoichiometric 1:1 complex with alpha-amylase. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. |
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