4c9l - Revision history

OCA at 12:06, 20 December 2023

OCA — Wed, 20 Dec 2023 12:06:17 GMT

←Older revision		Revision as of 12:06, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c9l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Novosphingobium_aromaticivorans Novosphingobium aromaticivorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C9L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C9L FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c9l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Novosphingobium_aromaticivorans Novosphingobium aromaticivorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C9L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C9L FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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]] 1.801Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=4c9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c9l OCA], [https://pdbe.org/4c9l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c9l RCSB], [https://www.ebi.ac.uk/pdbsum/4c9l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c9l 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=4c9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c9l OCA], [https://pdbe.org/4c9l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c9l RCSB], [https://www.ebi.ac.uk/pdbsum/4c9l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c9l ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/Q2GB12_NOVAD Q2GB12_NOVAD]]	+	[https://www.uniprot.org/uniprot/Q2GB12_NOVAD Q2GB12_NOVAD]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Although CYP101D1 and P450cam catalyze the same reaction at similar rates and share strikingly similar active site architectures, there are significant functional differences. CYP101D1 thus provides an opportunity to probe what structural and functional features must be shared and what features can differ but maintain the high catalytic efficiency. Crystal structures of the cyanide complex of wild-type CYP101D1 and it active site mutants, D259N and T260A, have been determined. The conformational changes in CYP101D1 upon cyanide binding are very similar to those of P450cam, indicating a similar mechanism for proton delivery during oxygen activation using solvent-assisted proton transfer. The D259N-CN- complex shows a perturbed solvent structure compared to that of the wild type, which is similar to what was observed in the oxy complex of the corresonding D251N mutant in P450cam. As in P450cam, the T260A mutant is highly uncoupled while the D259N mutant gives barely detectable activity. Despite these similarities, CYP101D1 is able to use the P450cam redox partners while P450cam cannot use the CYP101D1 redox partners. Thus, the strict requirement of P450cam for its own redox partner is relaxed in CYP101D1. Differences in the local environment of the essential Asp (Asp259 in CYP101D1) provide a strucutral basis for understanding these functional differences.
		+
		+	Crystal Structures and Functional Characterization of Wild-Type CYP101D1 and Its Active Site Mutants.,Batabyal D, Poulos TL Biochemistry. 2013 Nov 27. PMID:24261604<ref>PMID:24261604</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4c9l" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Cytochrome P450 3D structures\|Cytochrome P450 3D structures]]		*[[Cytochrome P450 3D structures\|Cytochrome P450 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 17:33, 7 September 2022

OCA — Wed, 07 Sep 2022 17:33:32 GMT

←Older revision		Revision as of 17:33, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4c9l' size='340' side='right'caption='[[4c9l]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='4c9l' size='340' side='right'caption='[[4c9l]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4c9l]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Atcc_700278 Atcc 700278~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C9L OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4C9L FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4c9l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Novosphingobium_aromaticivorans Novosphingobium aromaticivorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C9L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C9L FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c9k\|4c9k]], [[4c9m\|4c9m]], [[4c9n\|4c9n]], [[4c9o\|4c9o]], [[4c9p\|4c9p]]~~</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=4c9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c9l OCA], [https://pdbe.org/4c9l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c9l RCSB], [https://www.ebi.ac.uk/pdbsum/4c9l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c9l ProSAT]</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=4c9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c9l OCA], [~~http~~://pdbe.org/4c9l PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4c9l RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4c9l PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4c9l ProSAT]</span></td></tr>	+
	</table>		</table>
-	~~<div style~~=~~"background-color:#fffaf0;">~~	+	== Function ==
-	=~~= Publication Abstract from PubMed~~ ==	+	[[https://www.uniprot.org/uniprot/Q2GB12_NOVAD Q2GB12_NOVAD]]
-	Although CYP101D1 and P450cam catalyze the same reaction at similar rates and share strikingly similar active site architectures, there are significant functional differences. CYP101D1 thus provides an opportunity to probe what structural and functional features must be shared and what features can differ but maintain the high catalytic efficiency. Crystal structures of the cyanide complex of wild-type CYP101D1 and it active site mutants, D259N and T260A, have been determined. The conformational changes in CYP101D1 upon cyanide binding are very similar to those of P450cam, indicating a similar mechanism for proton delivery during oxygen activation using solvent-assisted proton transfer. The D259N-CN- complex shows a perturbed solvent structure compared to that of the wild type, which is similar to what was observed in the oxy complex of the corresonding D251N mutant in P450cam. As in P450cam, the T260A mutant is highly uncoupled while the D259N mutant gives barely detectable activity. Despite these similarities, CYP101D1 is able to use the P450cam redox partners while P450cam cannot use the CYP101D1 redox partners. Thus, the strict requirement of P450cam for its own redox partner is relaxed in CYP101D1. Differences in the local environment of the essential Asp (Asp259 in CYP101D1) provide a strucutral basis for understanding these functional differences.	+
-		+
-	~~Crystal Structures and Functional Characterization of Wild-Type CYP101D1 and Its Active Site Mutants.,Batabyal D, Poulos TL Biochemistry. 2013 Nov 27. PMID~~:~~24261604<ref>PMID:24261604<~~/~~ref>~~	+
-		+
-	~~From MEDLINE®~~/~~PubMed®, a database of the U~~.S. ~~National Library of Medicine.<br>~~	+
-	</~~div>~~	+
-	~~<div class="pdbe-citations 4c9l" style="background-color:#fffaf0;"><~~/~~div>~~	+

	==See Also==		==See Also==
-	*[[Cytochrome P450\|Cytochrome P450]]	+	*[[Cytochrome P450 3D structures\|Cytochrome P450 3D structures]]
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Atcc 700278]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Batabyal, D~~]]	+	[[Category: Novosphingobium aromaticivorans]]
-	[[Category: ~~Poulos, T L~~]]	+	[[Category: Batabyal D]]
-	[[Category: ~~Mono-oxygenase]]~~	+	[[Category: L Poulos T]]
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 08:44, 20 March 2019

OCA — Wed, 20 Mar 2019 08:44:29 GMT

←Older revision		Revision as of 08:44, 20 March 2019
Line 1:		Line 1:

	==Structure of Cyanide and Camphor bound wild type CYP101D1==		==Structure of Cyanide and Camphor bound wild type CYP101D1==
-	<StructureSection load='4c9l' size='340' side='right' caption='[[4c9l]], [[Resolution\|resolution]] 1.80Å' scene=''>	+	<StructureSection load='4c9l' size='340' side='right'caption='[[4c9l]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c9l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_700278 Atcc 700278]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C9L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C9L FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c9l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_700278 Atcc 700278]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C9L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C9L FirstGlance]. <br>
Line 25:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Atcc 700278]]		[[Category: Atcc 700278]]
		+	[[Category: Large Structures]]
	[[Category: Batabyal, D]]		[[Category: Batabyal, D]]
	[[Category: Poulos, T L]]		[[Category: Poulos, T L]]
	[[Category: Mono-oxygenase]]		[[Category: Mono-oxygenase]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 15:41, 5 August 2016

OCA — Fri, 05 Aug 2016 15:41:18 GMT

←Older revision		Revision as of 15:41, 5 August 2016
Line 1:		Line 1:
		+
	==Structure of Cyanide and Camphor bound wild type CYP101D1==		==Structure of Cyanide and Camphor bound wild type CYP101D1==
	<StructureSection load='4c9l' size='340' side='right' caption='[[4c9l]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='4c9l' size='340' side='right' caption='[[4c9l]], [[Resolution\|resolution]] 1.80Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c9k\|4c9k]], [[4c9m\|4c9m]], [[4c9n\|4c9n]], [[4c9o\|4c9o]], [[4c9p\|4c9p]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c9k\|4c9k]], [[4c9m\|4c9m]], [[4c9n\|4c9n]], [[4c9o\|4c9o]], [[4c9p\|4c9p]]</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=4c9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c9l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c9l RCSB], [http://www.ebi.ac.uk/pdbsum/4c9l 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=4c9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c9l OCA], [http://pdbe.org/4c9l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c9l RCSB], [http://www.ebi.ac.uk/pdbsum/4c9l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c9l ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 15:		Line 16:
	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 4c9l" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 16:12, 21 December 2014

OCA — Sun, 21 Dec 2014 16:12:29 GMT

←Older revision		Revision as of 16:12, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4c9l\| PDB=4c9l \| SCENE= }}~~	+	==Structure of Cyanide and Camphor bound wild type CYP101D1==
-	===Structure of Cyanide and Camphor bound wild type CYP101D1===	+	<StructureSection load='4c9l' size='340' side='right' caption='[[4c9l]], [[Resolution\|resolution]] 1.80Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24261604}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4c9l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_700278 Atcc 700278]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C9L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C9L FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c9k\|4c9k]], [[4c9m\|4c9m]], [[4c9n\|4c9n]], [[4c9o\|4c9o]], [[4c9p\|4c9p]]</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=4c9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c9l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c9l RCSB], [http://www.ebi.ac.uk/pdbsum/4c9l PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Although CYP101D1 and P450cam catalyze the same reaction at similar rates and share strikingly similar active site architectures, there are significant functional differences. CYP101D1 thus provides an opportunity to probe what structural and functional features must be shared and what features can differ but maintain the high catalytic efficiency. Crystal structures of the cyanide complex of wild-type CYP101D1 and it active site mutants, D259N and T260A, have been determined. The conformational changes in CYP101D1 upon cyanide binding are very similar to those of P450cam, indicating a similar mechanism for proton delivery during oxygen activation using solvent-assisted proton transfer. The D259N-CN- complex shows a perturbed solvent structure compared to that of the wild type, which is similar to what was observed in the oxy complex of the corresonding D251N mutant in P450cam. As in P450cam, the T260A mutant is highly uncoupled while the D259N mutant gives barely detectable activity. Despite these similarities, CYP101D1 is able to use the P450cam redox partners while P450cam cannot use the CYP101D1 redox partners. Thus, the strict requirement of P450cam for its own redox partner is relaxed in CYP101D1. Differences in the local environment of the essential Asp (Asp259 in CYP101D1) provide a strucutral basis for understanding these functional differences.

-	~~==About this Structure==~~	+	Crystal Structures and Functional Characterization of Wild-Type CYP101D1 and Its Active Site Mutants.,Batabyal D, Poulos TL Biochemistry. 2013 Nov 27. PMID:24261604<ref>PMID:24261604</ref>
-	~~[[4c9l]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Atcc_700278 Atcc 700278]~~. ~~Full crystallographic information is available from [http~~:/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=4C9L OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group~~=~~"xtra">PMID:024261604</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+
		+	==See Also==
		+	*[[Cytochrome P450\|Cytochrome P450]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Atcc 700278]]		[[Category: Atcc 700278]]
-	[[Category: Batabyal, D.]]	+	[[Category: Batabyal, D]]
-	[[Category: Poulos, T L.]]	+	[[Category: Poulos, T L]]
	[[Category: Mono-oxygenase]]		[[Category: Mono-oxygenase]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 08:31, 25 December 2013

OCA — Wed, 25 Dec 2013 08:31:23 GMT

←Older revision		Revision as of 08:31, 25 December 2013
Line 4:		Line 4:

	==About this Structure==		==About this Structure==
-	[[4c9l]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C9L OCA].	+	[[4c9l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_700278 Atcc 700278]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C9L OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:024261604</ref><references group="xtra"/><references/>		<ref group="xtra">PMID:024261604</ref><references group="xtra"/><references/>
		+	[[Category: Atcc 700278]]
	[[Category: Batabyal, D.]]		[[Category: Batabyal, D.]]
	[[Category: Poulos, T L.]]		[[Category: Poulos, T L.]]
	[[Category: Mono-oxygenase]]		[[Category: Mono-oxygenase]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 07:18, 4 December 2013

OCA — Wed, 04 Dec 2013 07:18:27 GMT

←Older revision		Revision as of 07:18, 4 December 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4c9l\| PDB=4c9l \| SCENE= }}
		+	===Structure of Cyanide and Camphor bound wild type CYP101D1===
		+	{{ABSTRACT_PUBMED_24261604}}

-	~~The entry~~ 4c9l is ~~ON HOLD until Paper Publication~~	+	==About this Structure==
		+	[[4c9l]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C9L OCA].

-	~~Authors~~: Batabyal, D.~~, L~~ Poulos, T.	+	==Reference==
-		+	<ref group="xtra">PMID:024261604</ref><references group="xtra"/><references/>
-	~~Description~~: ~~Structure of Cyanide and Camphor bound wild type CYP101D1~~	+	[[Category: Batabyal, D.]]
		+	[[Category: Poulos, T L.]]
		+	[[Category: Mono-oxygenase]]
		+	[[Category: Oxidoreductase]]

OCA: Protected "4c9l" [edit=sysop:move=sysop]

OCA — Thu, 10 Oct 2013 05:29:23 GMT

Protected "4c9l" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:29, 10 October 2013

OCA: New page: '''Unreleased structure''' The entry 4c9l is ON HOLD until Paper Publication Authors: Batabyal, D., L Poulos, T. Description: Structure of Cyanide and Camphor bound wild type CYP101D1

OCA — Thu, 10 Oct 2013 05:29:22 GMT

New page: '''Unreleased structure''' The entry 4c9l is ON HOLD until Paper Publication Authors: Batabyal, D., L Poulos, T. Description: Structure of Cyanide and Camphor bound wild type CYP101D1

New page

'''Unreleased structure'''

The entry 4c9l is ON HOLD until Paper Publication

Authors: Batabyal, D., L Poulos, T.

Description: Structure of Cyanide and Camphor bound wild type CYP101D1