1hoe: Difference between revisions

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[[Image:1hoe.png|left|200px]]
==CRYSTAL STRUCTURE DETERMINATION, REFINEMENT AND THE MOLECULAR MODEL OF THE ALPHA-AMYLASE INHIBITOR HOE-467A==
<StructureSection load='1hoe' size='340' side='right' caption='[[1hoe]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hoe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_tendae Streptomyces tendae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HOE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HOE FirstGlance]. <br>
</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=1hoe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hoe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hoe RCSB], [http://www.ebi.ac.uk/pdbsum/1hoe PDBsum]</span></td></tr>
<table>
== Evolutionary Conservation ==
[[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/ho/1hoe_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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal and molecular structure of the alpha-amylase inhibitor Hoe-467A has been determined and refined at high resolution. The polypeptide chain is folded in two triple-stranded sheets, which form a barrel. The topology of folding is as found in the immunoglobulin domains. The amino acid triplet Trp18-Arg19-Tyr20 has an exceptional conformation and position in the molecule and is possibly involved in inhibitory activity.


{{STRUCTURE_1hoe|  PDB=1hoe  |  SCENE=  }}
Crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor Hoe-467A.,Pflugrath JW, Wiegand G, Huber R, Vertesy L J Mol Biol. 1986 May 20;189(2):383-6. PMID:3489104<ref>PMID:3489104</ref>


===CRYSTAL STRUCTURE DETERMINATION, REFINEMENT AND THE MOLECULAR MODEL OF THE ALPHA-AMYLASE INHIBITOR HOE-467A===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_3489104}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[1hoe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_tendae Streptomyces tendae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HOE OCA].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:003489104</ref><ref group="xtra">PMID:011880627</ref><ref group="xtra">PMID:014695246</ref><ref group="xtra">PMID:017154716</ref><ref group="xtra">PMID:019113835</ref><references group="xtra"/>
[[Category: Streptomyces tendae]]
[[Category: Streptomyces tendae]]
[[Category: Huber, R.]]
[[Category: Huber, R.]]

Revision as of 17:16, 28 September 2014

CRYSTAL STRUCTURE DETERMINATION, REFINEMENT AND THE MOLECULAR MODEL OF THE ALPHA-AMYLASE INHIBITOR HOE-467ACRYSTAL STRUCTURE DETERMINATION, REFINEMENT AND THE MOLECULAR MODEL OF THE ALPHA-AMYLASE INHIBITOR HOE-467A

Structural highlights

1hoe is a 1 chain structure with sequence from Streptomyces tendae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, RCSB, PDBsum

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 PubMed

The crystal and molecular structure of the alpha-amylase inhibitor Hoe-467A has been determined and refined at high resolution. The polypeptide chain is folded in two triple-stranded sheets, which form a barrel. The topology of folding is as found in the immunoglobulin domains. The amino acid triplet Trp18-Arg19-Tyr20 has an exceptional conformation and position in the molecule and is possibly involved in inhibitory activity.

Crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor Hoe-467A.,Pflugrath JW, Wiegand G, Huber R, Vertesy L J Mol Biol. 1986 May 20;189(2):383-6. PMID:3489104[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Pflugrath JW, Wiegand G, Huber R, Vertesy L. Crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor Hoe-467A. J Mol Biol. 1986 May 20;189(2):383-6. PMID:3489104

1hoe, resolution 2.00Å

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