1c9m

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1c9m" [edit=sysop:move=sysop])
Current revision (21:56, 26 March 2025) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1c9m.png|left|200px]]
 
-
<!--
+
==BACILLUS LENTUS SUBTILSIN (SER 87) N76D/S103A/V104I==
-
The line below this paragraph, containing "STRUCTURE_1c9m", creates the "Structure Box" on the page.
+
<StructureSection load='1c9m' size='340' side='right'caption='[[1c9m]], [[Resolution|resolution]] 1.67&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'>[[1c9m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lederbergia_lenta Lederbergia lenta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C9M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C9M 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]] 1.67&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SEB:O-BENZYLSULFONYL-SERINE'>SEB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
{{STRUCTURE_1c9m| PDB=1c9m | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1c9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c9m OCA], [https://pdbe.org/1c9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c9m RCSB], [https://www.ebi.ac.uk/pdbsum/1c9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c9m ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/SUBS_LEDLE SUBS_LEDLE] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
 +
== 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/c9/1c9m_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1c9m ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The three-dimensional structures of engineered variants of Bacillus lentus subtilisin having increased enzymatic activity, K27R/N87S/V104Y/N123S/T274A (RSYSA) and N76D/N87S/S103A/V104I (DSAI), were determined by X-ray crystallography. In addition to identifying changes in atomic position we report a method that identifies protein segments having altered flexibility. The method utilizes a statistical analysis of variance to delineate main-chain temperature factors that represent significant departures from the overall variance between equivalent regions seen throughout the structure. This method reveals changes in main-chain mobility in both variants. Residues 125-127 have increased mobility in the RSYSA variant while residues 100-104 have decreased mobility in the DSAI variant. These segments are located at the substrate-binding site and changes in their mobility are believed to relate to the observed changes in proteolytic activity. The effect of altered crystal lattice contacts on segment flexibility becomes apparent when identical variants, determined in two crystal forms, are compared with the native enzyme.
-
===BACILLUS LENTUS SUBTILSIN (SER 87) N76D/S103A/V104I===
+
Engineered Bacillus lentus subtilisins having altered flexibility.,Graycar T, Knapp M, Ganshaw G, Dauberman J, Bott R J Mol Biol. 1999 Sep 10;292(1):97-109. PMID:10493860<ref>PMID:10493860</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_10493860}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 1c9m" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 10493860 is the PubMed ID number.
+
-
-->
+
-
{{ABSTRACT_PUBMED_10493860}}
+
-
 
+
-
==About this Structure==
+
-
[[1c9m]] is a 1 chain structure of [[Subtilisin]] with sequence from [http://en.wikipedia.org/wiki/Bacillus_lentus Bacillus lentus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C9M OCA].
+
==See Also==
==See Also==
-
*[[Subtilisin]]
+
*[[Subtilisin 3D structures|Subtilisin 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:10493860</ref><references group="xtra"/>
+
__TOC__
-
[[Category: Bacillus lentus]]
+
</StructureSection>
-
[[Category: Subtilisin]]
+
[[Category: Large Structures]]
-
[[Category: Bott, R.]]
+
[[Category: Lederbergia lenta]]
-
[[Category: Altered flexibility]]
+
[[Category: Bott R]]
-
[[Category: Hydrolase]]
+
-
[[Category: Serine protease]]
+
-
[[Category: Site-specific variant]]
+
-
[[Category: Subtilisin]]
+

Current revision

BACILLUS LENTUS SUBTILSIN (SER 87) N76D/S103A/V104I

PDB ID 1c9m

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1c9m"
Personal tools