1k17

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{{Theoretical_model}}
{{Theoretical_model}}
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{{Seed}}
 
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[[Image:1k17.png|left|200px]]
 
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==ALIPHATIC AMIDASE (EC 3.5.1.4)==
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The line below this paragraph, containing "STRUCTURE_1k17", creates the "Structure Box" on the page.
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<StructureSection load='1k17' size='340' side='right'caption='[[1k17]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K17 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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=1k17 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1k17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k17 ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_1k17| PDB=1k17 | SCENE= }}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The aliphatic amidase from Pseudomonas aeruginosa belongs to the nitrilase superfamily, and Cys(166) is the nucleophile of the catalytic mechanism. A model of amidase was built by comparative modelling using the crystal structure of the worm nitrilase-fragile histidine triad fusion protein (NitFhit; Protein Data Bank accession number 1EMS) as a template. The amidase model predicted a catalytic triad (Cys-Glu-Lys) situated at the bottom of a pocket and identical with the presumptive catalytic triad of NitFhit. Three-dimensional models for other amidases belonging to the nitrilase superfamily also predicted Cys-Glu-Lys catalytic triads. Support for the structure for the P. aeruginosa amidase came from site-direct mutagenesis and from the locations of amino acid residues that altered substrate specificity or binding when mutated.
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===ALIPHATIC AMIDASE (EC 3.5.1.4)===
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Support for a three-dimensional structure predicting a Cys-Glu-Lys catalytic triad for Pseudomonas aeruginosa amidase comes from site-directed mutagenesis and mutations altering substrate specificity.,Novo C, Farnaud S, Tata R, Clemente A, Brown PR Biochem J. 2002 Aug 1;365(Pt 3):731-8. PMID:11955282<ref>PMID:11955282</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_11955282}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1k17" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 11955282 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11955282}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Theoretical Model]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K17 OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:11955282</ref><references group="xtra"/>
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[[Category: Brown, P R]]
[[Category: Brown, P R]]
[[Category: Clemente, A]]
[[Category: Clemente, A]]
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[[Category: Novo, C]]
[[Category: Novo, C]]
[[Category: Tata, R]]
[[Category: Tata, R]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 06:59:52 2010''
 

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

ALIPHATIC AMIDASE (EC 3.5.1.4)

PDB ID 1k17

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