2b5d: Difference between revisions

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[[Image:2b5d.png|left|200px]]


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==Crystal structure of the novel alpha-amylase AmyC from Thermotoga maritima==
The line below this paragraph, containing "STRUCTURE_2b5d", creates the "Structure Box" on the page.
<StructureSection load='2b5d' size='340' side='right'caption='[[2b5d]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2b5d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B5D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B5D FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2b5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b5d OCA], [https://pdbe.org/2b5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b5d RCSB], [https://www.ebi.ac.uk/pdbsum/2b5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b5d ProSAT]</span></td></tr>
{{STRUCTURE_2b5d|  PDB=2b5d |  SCENE= }}
</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/b5/2b5d_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=2b5d ConSurf].
<div style="clear:both"></div>


===Crystal structure of the novel alpha-amylase AmyC from Thermotoga maritima===
==See Also==
 
*[[Amylase 3D structures|Amylase 3D structures]]
 
__TOC__
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</StructureSection>
The line below this paragraph, {{ABSTRACT_PUBMED_16510973}}, adds the Publication Abstract to the page
[[Category: Large Structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 16510973 is the PubMed ID number.
[[Category: Thermotoga maritima MSB8]]
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[[Category: Ballschmiter M]]
{{ABSTRACT_PUBMED_16510973}}
[[Category: Dickmanns A]]
 
[[Category: Ficner R]]
==About this Structure==
[[Category: Liebl W]]
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B5D OCA].
 
==Reference==
Structure of the novel alpha-amylase AmyC from Thermotoga maritima., Dickmanns A, Ballschmiter M, Liebl W, Ficner R, Acta Crystallogr D Biol Crystallogr. 2006 Mar;62(Pt 3):262-70. Epub 2006, Feb 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16510973 16510973]
[[Category: Alpha-amylase]]
[[Category: Ballschmiter, M.]]
[[Category: Dickmanns, A.]]
[[Category: Ficner, R.]]
[[Category: Liebl, W.]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:47:55 2008''

Latest revision as of 16:42, 13 March 2024

Crystal structure of the novel alpha-amylase AmyC from Thermotoga maritimaCrystal structure of the novel alpha-amylase AmyC from Thermotoga maritima

Structural highlights

2b5d is a 1 chain structure with sequence from Thermotoga maritima MSB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2b5d, resolution 2.20Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
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