4f60 - Revision history

OCA at 15:17, 14 March 2024

OCA — Thu, 14 Mar 2024 15:17:04 GMT

←Older revision		Revision as of 15:17, 14 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4f60]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_rhodochrous Rhodococcus rhodochrous]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F60 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4f60]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_rhodochrous Rhodococcus rhodochrous]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F60 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F:FLUORIDE+ION'>F</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.45Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F:FLUORIDE+ION'>F</scene></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=4f60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f60 OCA], [https://pdbe.org/4f60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f60 RCSB], [https://www.ebi.ac.uk/pdbsum/4f60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f60 ProSAT]</span></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=4f60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f60 OCA], [https://pdbe.org/4f60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f60 RCSB], [https://www.ebi.ac.uk/pdbsum/4f60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f60 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/DHAA_RHORH DHAA_RHORH] Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Expresses halogenase activity against 1-chloroalkanes of chain length C3 to C10, and also shows a very weak activity with 1,2-dichloroethane.		[https://www.uniprot.org/uniprot/DHAA_RHORH DHAA_RHORH] Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Expresses halogenase activity against 1-chloroalkanes of chain length C3 to C10, and also shows a very weak activity with 1,2-dichloroethane.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Mutations targeting as few as four residues lining the access tunnel extended the half-life of an enzyme in 40 % dimethyl sulfoxide from minutes to weeks and increased its melting temperature by 190 degrees C. Protein crystallography and molecular dynamics revealed that the tunnel residue packing is a key determinant of protein stability and the active-site accessibility for cosolvent molecules (red dots).
-
-	Engineering Enzyme Stability and Resistance to an Organic Cosolvent by Modification of Residues in the Access Tunnel.,Koudelakova T, Chaloupkova R, Brezovsky J, Prokop Z, Sebestova E, Hesseler M, Khabiri M, Plevaka M, Kulik D, Kuta Smatanova I, Rezacova P, Ettrich R, Bornscheuer UT, Damborsky J Angew Chem Int Ed Engl. 2013 Jan 9. doi: 10.1002/anie.201206708. PMID:23303607<ref>PMID:23303607</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4f60" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Dehalogenase 3D structures\|Dehalogenase 3D structures]]		*[[Dehalogenase 3D structures\|Dehalogenase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 04:37, 7 October 2022

OCA — Fri, 07 Oct 2022 04:37:07 GMT

←Older revision		Revision as of 04:37, 7 October 2022
Line 1:		Line 1:

	==Crystal structure of Rhodococcus rhodochrous haloalkane dehalogenase mutant (T148L, G171Q, A172V, C176F).==		==Crystal structure of Rhodococcus rhodochrous haloalkane dehalogenase mutant (T148L, G171Q, A172V, C176F).==
-	<StructureSection load='4f60' size='340' side='right' caption='[[4f60]], [[Resolution\|resolution]] 1.45Å' scene=''>	+	<StructureSection load='4f60' size='340' side='right'caption='[[4f60]], [[Resolution\|resolution]] 1.45Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4f60]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~"bacterium_mycoides_roseum"_grotenfelt_1889 "bacterium mycoides roseum" grotenfelt 1889~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F60 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4F60 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4f60]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_rhodochrous Rhodococcus rhodochrous]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F60 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F:FLUORIDE+ION'>F</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F:FLUORIDE+ION'>F</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dhaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1829 "Bacterium mycoides roseum" Grotenfelt 1889])</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=4f60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f60 OCA], [https://pdbe.org/4f60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f60 RCSB], [https://www.ebi.ac.uk/pdbsum/4f60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f60 ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Haloalkane_dehalogenase Haloalkane dehalogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.5 3.8.1.5] </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=4f60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f60 OCA], [~~http~~://pdbe.org/4f60 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4f60 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4f60 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4f60 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/DHAA_RHORH DHAA_RHORH]] Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Expresses halogenase activity against 1-chloroalkanes of chain length C3 to C10, and also shows a very weak activity with 1,2-dichloroethane.	+	[https://www.uniprot.org/uniprot/DHAA_RHORH DHAA_RHORH] Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Expresses halogenase activity against 1-chloroalkanes of chain length C3 to C10, and also shows a very weak activity with 1,2-dichloroethane.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 20:

	==See Also==		==See Also==
-	*[[Dehalogenase\|Dehalogenase]]	+	*[[Dehalogenase 3D structures\|Dehalogenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacterium mycoides roseum grotenfelt 1889~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Haloalkane dehalogenase~~]]	+	[[Category: Rhodococcus rhodochrous]]
-	[[Category: Kuta-Smatanova, I]]	+	[[Category: Kuta-Smatanova I]]
-	[[Category: Plevaka, M]]	+	[[Category: Plevaka M]]
-	[[Category: Rezacova, P]]	+	[[Category: Rezacova P]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Mutation in access tunnel~~]]	+

OCA at 20:17, 5 August 2016

OCA — Fri, 05 Aug 2016 20:17:21 GMT

←Older revision		Revision as of 20:17, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of Rhodococcus rhodochrous haloalkane dehalogenase mutant (T148L, G171Q, A172V, C176F).==		==Crystal structure of Rhodococcus rhodochrous haloalkane dehalogenase mutant (T148L, G171Q, A172V, C176F).==
	<StructureSection load='4f60' size='340' side='right' caption='[[4f60]], [[Resolution\|resolution]] 1.45Å' scene=''>		<StructureSection load='4f60' size='340' side='right' caption='[[4f60]], [[Resolution\|resolution]] 1.45Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4f60]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Rhodococcus_rhodochrous Rhodococcus rhodochrous~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F60 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F60 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4f60]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_mycoides_roseum"_grotenfelt_1889 "bacterium mycoides roseum" grotenfelt 1889]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F60 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F60 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F:FLUORIDE+ION'>F</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F:FLUORIDE+ION'>F</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dhaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1829 ~~Rhodococcus rhodochrous~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dhaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1829 "Bacterium mycoides roseum" Grotenfelt 1889])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Haloalkane_dehalogenase Haloalkane dehalogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.5 3.8.1.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Haloalkane_dehalogenase Haloalkane dehalogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.5 3.8.1.5] </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=4f60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f60 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f60 RCSB], [http://www.ebi.ac.uk/pdbsum/4f60 PDBsum]</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=4f60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f60 OCA], [http://pdbe.org/4f60 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4f60 RCSB], [http://www.ebi.ac.uk/pdbsum/4f60 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4f60 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4f60" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 25:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Bacterium mycoides roseum grotenfelt 1889]]
	[[Category: Haloalkane dehalogenase]]		[[Category: Haloalkane dehalogenase]]
-	[[Category: Rhodococcus rhodochrous]]
	[[Category: Kuta-Smatanova, I]]		[[Category: Kuta-Smatanova, I]]
	[[Category: Plevaka, M]]		[[Category: Plevaka, M]]

OCA at 21:34, 25 December 2014

OCA — Thu, 25 Dec 2014 21:34:49 GMT

←Older revision		Revision as of 21:34, 25 December 2014
Line 8:		Line 8:
	<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=4f60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f60 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f60 RCSB], [http://www.ebi.ac.uk/pdbsum/4f60 PDBsum]</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=4f60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f60 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f60 RCSB], [http://www.ebi.ac.uk/pdbsum/4f60 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DHAA_RHORH DHAA_RHORH]] Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Expresses halogenase activity against 1-chloroalkanes of chain length C3 to C10, and also shows a very weak activity with 1,2-dichloroethane.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 17:07, 9 December 2014

OCA — Tue, 09 Dec 2014 17:07:55 GMT

←Older revision		Revision as of 17:07, 9 December 2014
Line 1:		Line 1:
-	[[~~Image:~~4f60.~~png~~\|~~left~~\|~~200px~~]]	+	==Crystal structure of Rhodococcus rhodochrous haloalkane dehalogenase mutant (T148L, G171Q, A172V, C176F).==
		+	<StructureSection load='4f60' size='340' side='right' caption='[[4f60]], [[Resolution\|resolution]] 1.45Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4f60]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodococcus_rhodochrous Rhodococcus rhodochrous]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F60 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F60 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F:FLUORIDE+ION'>F</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dhaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1829 Rhodococcus rhodochrous])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Haloalkane_dehalogenase Haloalkane dehalogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.5 3.8.1.5] </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=4f60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f60 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f60 RCSB], [http://www.ebi.ac.uk/pdbsum/4f60 PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Mutations targeting as few as four residues lining the access tunnel extended the half-life of an enzyme in 40 % dimethyl sulfoxide from minutes to weeks and increased its melting temperature by 190 degrees C. Protein crystallography and molecular dynamics revealed that the tunnel residue packing is a key determinant of protein stability and the active-site accessibility for cosolvent molecules (red dots).

-	~~{{STRUCTURE_4f60\| PDB=4f60 \| SCENE= }}~~	+	Engineering Enzyme Stability and Resistance to an Organic Cosolvent by Modification of Residues in the Access Tunnel.,Koudelakova T, Chaloupkova R, Brezovsky J, Prokop Z, Sebestova E, Hesseler M, Khabiri M, Plevaka M, Kulik D, Kuta Smatanova I, Rezacova P, Ettrich R, Bornscheuer UT, Damborsky J Angew Chem Int Ed Engl. 2013 Jan 9. doi: 10.1002/anie.201206708. PMID:23303607<ref>PMID:23303607</ref>

-	~~===Crystal structure of Rhodococcus rhodochrous haloalkane dehalogenase mutant (T148L~~, ~~G171Q, A172V, C176F)~~.~~===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_23303607}}~~	+	==See Also==
-		+	*[[Dehalogenase\|Dehalogenase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~4f60~~]] ~~is a 1 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Rhodococcus_rhodochrous Rhodococcus rhodochrous]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F60 OCA].~~	+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Haloalkane dehalogenase]]		[[Category: Haloalkane dehalogenase]]
	[[Category: Rhodococcus rhodochrous]]		[[Category: Rhodococcus rhodochrous]]
-	[[Category: Kuta-Smatanova, I.]]	+	[[Category: Kuta-Smatanova, I]]
-	[[Category: Plevaka, M.]]	+	[[Category: Plevaka, M]]
-	[[Category: Rezacova, P.]]	+	[[Category: Rezacova, P]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Mutation in access tunnel]]		[[Category: Mutation in access tunnel]]

OCA at 14:00, 27 February 2013

OCA — Wed, 27 Feb 2013 14:00:08 GMT

←Older revision		Revision as of 14:00, 27 February 2013
Line 1:		Line 1:
-	[[Image:4f60.~~jpg~~\|left\|200px]]	+	[[Image:4f60.png\|left\|200px]]

	{{STRUCTURE_4f60\| PDB=4f60 \| SCENE= }}		{{STRUCTURE_4f60\| PDB=4f60 \| SCENE= }}

OCA at 11:52, 23 January 2013

OCA — Wed, 23 Jan 2013 11:52:26 GMT

←Older revision		Revision as of 11:52, 23 January 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4f60.jpg\|left\|200px]]

-	~~The entry~~ 4f60 ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_4f60\| PDB=4f60 \| SCENE= }}

-	~~Authors: Plevaka~~, ~~M., Kuta-Smatanova, I.~~, ~~Rezacova~~, P.	+	===Crystal structure of Rhodococcus rhodochrous haloalkane dehalogenase mutant (T148L, G171Q, A172V, C176F).===

-	~~Description: Crystal~~ structure of Rhodococcus rhodochrous ~~haloalkane~~ dehalogenase ~~mutant (T148L~~, ~~G171Q~~, ~~A172V~~, ~~C176F)~~.	+	{{ABSTRACT_PUBMED_23303607}}
		+
		+	==About this Structure==
		+	[[4f60]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodococcus_rhodochrous Rhodococcus rhodochrous]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F60 OCA].
		+	[[Category: Haloalkane dehalogenase]]
		+	[[Category: Rhodococcus rhodochrous]]
		+	[[Category: Kuta-Smatanova, I.]]
		+	[[Category: Plevaka, M.]]
		+	[[Category: Rezacova, P.]]
		+	[[Category: Hydrolase]]
		+	[[Category: Mutation in access tunnel]]

OCA at 05:47, 13 June 2012

OCA — Wed, 13 Jun 2012 05:47:21 GMT

←Older revision		Revision as of 05:47, 13 June 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4f60 is ON HOLD	+	The entry 4f60 is ON HOLD until Paper Publication

	Authors: Plevaka, M., Kuta-Smatanova, I., Rezacova, P.		Authors: Plevaka, M., Kuta-Smatanova, I., Rezacova, P.

	Description: Crystal structure of Rhodococcus rhodochrous haloalkane dehalogenase mutant (T148L, G171Q, A172V, C176F).		Description: Crystal structure of Rhodococcus rhodochrous haloalkane dehalogenase mutant (T148L, G171Q, A172V, C176F).

OCA at 07:19, 6 June 2012

OCA — Wed, 06 Jun 2012 07:19:21 GMT

←Older revision		Revision as of 07:19, 6 June 2012
Line 3:		Line 3:
	The entry 4f60 is ON HOLD		The entry 4f60 is ON HOLD

-	Authors: Plevaka, M. , Kuta Smatanova, I., Rezacova, P.	+	Authors: Plevaka, M., Kuta-Smatanova, I., Rezacova, P.

	Description: Crystal structure of Rhodococcus rhodochrous haloalkane dehalogenase mutant (T148L, G171Q, A172V, C176F).		Description: Crystal structure of Rhodococcus rhodochrous haloalkane dehalogenase mutant (T148L, G171Q, A172V, C176F).

OCA: Protected "4f60" [edit=sysop:move=sysop]

OCA — Wed, 23 May 2012 05:43:15 GMT

Protected "4f60" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:43, 23 May 2012