5apr: Difference between revisions

No edit summary
No edit summary
 
(7 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{Seed}}
[[Image:5apr.png|left|200px]]


<!--
==STRUCTURES OF COMPLEXES OF RHIZOPUSPEPSIN WITH PEPSTATIN AND OTHER STATINE-CONTAINING INHIBITORS==
The line below this paragraph, containing "STRUCTURE_5apr", creates the "Structure Box" on the page.
<StructureSection load='5apr' size='340' side='right'caption='[[5apr]], [[Resolution|resolution]] 2.10&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'>[[5apr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_52807 Atcc 52807]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5APR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5APR FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-->
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DHL:2-AMINO-ETHANETHIOL'>DHL</scene>, <scene name='pdbligand=STA:STATINE'>STA</scene></td></tr>
{{STRUCTURE_5apr|  PDB=5apr  |  SCENE=  }}
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4apr|4apr]], [[6apr|6apr]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.103, 3.4.23.18, 3.4.23.19, 3.4.23.20, 3.4.23.21, 3.4.23.22, 3.4.23.23, 3.4.23.24, 3.4.23.25, 3.4.23.26, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.19, 3.4.23.20, 3.4.23.21, 3.4.23.22, 3.4.23.23, 3.4.23.24, 3.4.23.25, 3.4.23.26, 3.4.23.28 and 3.4.23.30] </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=5apr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5apr OCA], [http://pdbe.org/5apr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5apr RCSB], [http://www.ebi.ac.uk/pdbsum/5apr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5apr ProSAT]</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/ap/5apr_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=5apr ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional structures of the complexes of the aspartic proteinase from Rhizopus chinensis (Rhizopuspepsin, EC 3.4.23.6) with pepstatin and two pepstatin-like peptide inhibitors of renin have been determined by X-ray diffraction methods and refined by restrained least-squares procedures. The inhibitors adopt an extended conformation and lie in the deep groove located between the two domains of the enzyme. Inhibitor binding is accompanied by a conformational change at the "flap," a beta-hairpin loop region, that projects over the binding cleft and closes down over the inhibitor, excluding water molecules from the vicinity of the scissile bond. The hydroxyl group of the central statyl residue of the inhibitors replaces the water molecule found between the two active aspartates, Asp-35 and Asp-218, in the native structure. The refined structures provide additional data to define the specific subsites of the enzyme and also show a system of hydrogen bonding to the inhibitor backbone similar to that observed for a reduced inhibitor.


===STRUCTURES OF COMPLEXES OF RHIZOPUSPEPSIN WITH PEPSTATIN AND OTHER STATINE-CONTAINING INHIBITORS===
Structures of complexes of rhizopuspepsin with pepstatin and other statine-containing inhibitors.,Suguna K, Padlan EA, Bott R, Boger J, Parris KD, Davies DR Proteins. 1992 Jul;13(3):195-205. PMID:1603809<ref>PMID:1603809</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5apr" style="background-color:#fffaf0;"></div>


<!--
==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_1603809}}, adds the Publication Abstract to the page
*[[Pepsin|Pepsin]]
(as it appears on PubMed at http://www.pubmed.gov), where 1603809 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_1603809}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Atcc 52807]]
5APR is a 2 chains structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5APR OCA].
 
==Reference==
<ref group="xtra">PMID:1603809</ref><references group="xtra"/>
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Davies, D R.]]
[[Category: Large Structures]]
[[Category: Suguna, K.]]
[[Category: Davies, D R]]
 
[[Category: Suguna, K]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 19:52:07 2009''
[[Category: Acid proteinase]]
[[Category: Hydrolase-hydrolase inhibitor complex]]

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

OCA