4nfk - Revision history

OCA at 16:55, 20 September 2023

OCA — Wed, 20 Sep 2023 16:55:43 GMT

←Older revision		Revision as of 16:55, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4nfk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NFK FirstGlance]. <br>		<table><tr><td colspan='2'>[[4nfk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NFK FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=JD5:[({5-[4-(CYCLOPROPYLOXY)PHENYL]PYRIDIN-3-YL}AMINO)METHANEDIYL]BIS(PHOSPHONIC+ACID)'>JD5</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.85Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=JD5:[({5-[4-(CYCLOPROPYLOXY)PHENYL]PYRIDIN-3-YL}AMINO)METHANEDIYL]BIS(PHOSPHONIC+ACID)'>JD5</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4nfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nfk OCA], [https://pdbe.org/4nfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nfk RCSB], [https://www.ebi.ac.uk/pdbsum/4nfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nfk 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=4nfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nfk OCA], [https://pdbe.org/4nfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nfk RCSB], [https://www.ebi.ac.uk/pdbsum/4nfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nfk ProSAT]</span></td></tr>
	</table>		</table>

OCA at 08:26, 11 January 2023

OCA — Wed, 11 Jan 2023 08:26:32 GMT

←Older revision		Revision as of 08:26, 11 January 2023
Line 3:		Line 3:
	<StructureSection load='4nfk' size='340' side='right'caption='[[4nfk]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='4nfk' size='340' side='right'caption='[[4nfk]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4nfk]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NFK OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4NFK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4nfk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NFK FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=JD5:[({5-[4-(CYCLOPROPYLOXY)PHENYL]PYRIDIN-3-YL}AMINO)METHANEDIYL]BIS(PHOSPHONIC+ACID)'>JD5</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=JD5:[({5-[4-(CYCLOPROPYLOXY)PHENYL]PYRIDIN-3-YL}AMINO)METHANEDIYL]BIS(PHOSPHONIC+ACID)'>JD5</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4nfi\|4nfi]], [[4nfj\|4nfj]]~~</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=4nfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nfk OCA], [https://pdbe.org/4nfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nfk RCSB], [https://www.ebi.ac.uk/pdbsum/4nfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nfk 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=4nfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nfk OCA], [~~http~~://pdbe.org/4nfk PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4nfk RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4nfk PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4nfk ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/FPPS_HUMAN FPPS_HUMAN]] Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate.	+	[https://www.uniprot.org/uniprot/FPPS_HUMAN FPPS_HUMAN] Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Berghuis~~, A M~~]]	+	[[Category: Berghuis AM]]
-	[[Category: ~~Park, J~~]]	+	[[Category: De schutter JW]]
-	[[Category: ~~Tsantrizos, Y S]]~~	+	[[Category: Park J]]
-	~~[[Category: Schutter,~~ J ~~W.De~~]]	+	[[Category: Tsantrizos YS]]
-	[[Category: ~~Transferase-transferase inhibitor complex~~]]	+

OCA at 17:51, 14 August 2019

OCA — Wed, 14 Aug 2019 17:51:21 GMT

←Older revision		Revision as of 17:51, 14 August 2019
Line 1:		Line 1:

	==Crystal structure of human FPPS in complex with nickel, JDS05120, and sulfate==		==Crystal structure of human FPPS in complex with nickel, JDS05120, and sulfate==
-	<StructureSection load='4nfk' size='340' side='right' caption='[[4nfk]], [[Resolution\|resolution]] 1.85Å' scene=''>	+	<StructureSection load='4nfk' size='340' side='right'caption='[[4nfk]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4nfk]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NFK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NFK FirstGlance]. <br>		<table><tr><td colspan='2'>[[4nfk]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NFK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NFK FirstGlance]. <br>
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 4nfk" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4nfk" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Farnesyl diphosphate synthase 3D structures\|Farnesyl diphosphate synthase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Berghuis, A M]]		[[Category: Berghuis, A M]]
	[[Category: Park, J]]		[[Category: Park, J]]

OCA at 06:54, 25 October 2017

OCA — Wed, 25 Oct 2017 06:54:05 GMT

←Older revision		Revision as of 06:54, 25 October 2017
Line 10:		Line 10:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/FPPS_HUMAN FPPS_HUMAN]] Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate.		[[http://www.uniprot.org/uniprot/FPPS_HUMAN FPPS_HUMAN]] Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Human farnesyl pyrophosphate synthase (hFPPS) catalyzes the production of the 15-carbon isoprenoid farnesyl pyrophosphate. The enzyme is a key regulator of the mevalonate pathway and a well-established drug target. Notably, it was elucidated as the molecular target of nitrogen-containing bisphosphonates, a class of drugs that have been widely successful against bone resorption disorders. More recently, research has focused on the anticancer effects of these inhibitors. In order to achieve increased non-skeletal tissue exposure, we created phenylaminopyridine bisphosphonates (PNP-BPs) that have bulky hydrophobic side chains through a structure-based approach. Some of these compounds have proven to be more potent than the current clinical drugs in a number of antiproliferation assays using multiple myeloma cell lines. In the present work, we characterized the binding of our most potent PNP-BPs to the target enzyme, hFPPS. Co-crystal structures demonstrate that the molecular interactions designed to elicit tighter binding are indeed established. We carried out thermodynamic studies as well; the newly introduced protein-ligand interactions are clearly reflected in the enthalpy of binding measured, which is more favorable for the new PNP-BPs than for the lead compound. These studies also indicate that the affinity of the PNP-BPs to hFPPS is comparable to that of the current drug risedronate. Risedronate forms additional polar interactions via its hydroxyl functional group and thus exhibits more favorable binding enthalpy; however, the entropy of binding is more favorable for the PNP-BPs, owing to the greater desolvation effects resulting from their large hydrophobic side chains. These results therefore confirm the overall validity of our drug design strategy. With a distinctly different molecular scaffold, the PNP-BPs described in this report represent an interesting new group of future drug candidates. Further investigation should follow to characterize the tissue distribution profile and assess the potential clinical benefits of these compounds.

-	==~~See Also~~==	+	Crystallographic and thermodynamic characterization of phenylaminopyridine bisphosphonates binding to human farnesyl pyrophosphate synthase.,Park J, Rodionov D, De Schutter JW, Lin YS, Tsantrizos YS, Berghuis AM PLoS One. 2017 Oct 16;12(10):e0186447. doi: 10.1371/journal.pone.0186447., eCollection 2017. PMID:29036218<ref>PMID:29036218</ref>
-	*[[Farnesyl diphosphate synthase\|Farnesyl diphosphate synthase]]	+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4nfk" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 08:16, 5 August 2016

OCA — Fri, 05 Aug 2016 08:16:48 GMT

←Older revision		Revision as of 08:16, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of human FPPS in complex with nickel, JDS05120, and sulfate==		==Crystal structure of human FPPS in complex with nickel, JDS05120, and sulfate==
	<StructureSection load='4nfk' size='340' side='right' caption='[[4nfk]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='4nfk' size='340' side='right' caption='[[4nfk]], [[Resolution\|resolution]] 1.85Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=JD5:[({5-[4-(CYCLOPROPYLOXY)PHENYL]PYRIDIN-3-YL}AMINO)METHANEDIYL]BIS(PHOSPHONIC+ACID)'>JD5</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=JD5:[({5-[4-(CYCLOPROPYLOXY)PHENYL]PYRIDIN-3-YL}AMINO)METHANEDIYL]BIS(PHOSPHONIC+ACID)'>JD5</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4nfi\|4nfi]], [[4nfj\|4nfj]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4nfi\|4nfi]], [[4nfj\|4nfj]]</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=4nfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nfk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nfk RCSB], [http://www.ebi.ac.uk/pdbsum/4nfk 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=4nfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nfk OCA], [http://pdbe.org/4nfk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nfk RCSB], [http://www.ebi.ac.uk/pdbsum/4nfk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nfk ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/FPPS_HUMAN FPPS_HUMAN]] Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate.		[[http://www.uniprot.org/uniprot/FPPS_HUMAN FPPS_HUMAN]] Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate.
		+
		+	==See Also==
		+	*[[Farnesyl diphosphate synthase\|Farnesyl diphosphate synthase]]
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 14:50, 31 December 2014

OCA — Wed, 31 Dec 2014 14:50:11 GMT

←Older revision		Revision as of 14:50, 31 December 2014
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal structure of human FPPS in complex with nickel, JDS05120, and sulfate==
-		+	<StructureSection load='4nfk' size='340' side='right' caption='[[4nfk]], [[Resolution\|resolution]] 1.85Å' scene=''>
-	~~The entry~~ 4nfk is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4nfk]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NFK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NFK FirstGlance]. <br>
-	~~Authors~~: ~~Park~~, J., ~~De schutter, J~~.W., ~~Tsantrizos, Y~~.S., ~~Berghuis, A~~.M.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=JD5:[({5-[4-(CYCLOPROPYLOXY)PHENYL]PYRIDIN-3-YL}AMINO)METHANEDIYL]BIS(PHOSPHONIC+ACID)'>JD5</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4nfi\|4nfi]], [[4nfj\|4nfj]]</td></tr>
-	~~Description~~: ~~Crystal structure of human FPPS~~ in ~~complex~~ with ~~nickel~~, ~~JDS05120~~, and ~~sulfate~~	+	<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=4nfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nfk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nfk RCSB], [http://www.ebi.ac.uk/pdbsum/4nfk PDBsum]</span></td></tr>
-	~~[[Category: Unreleased Structures]]~~	+	</table>
-	[[Category: ~~De Schutter~~, ~~J.W~~]]	+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FPPS_HUMAN FPPS_HUMAN]] Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate.
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Berghuis, A M]]
	[[Category: Park, J]]		[[Category: Park, J]]
-	[[Category: ~~Berghuis~~, ~~A.M~~]]	+	[[Category: Tsantrizos, Y S]]
-	[[Category: ~~Tsantrizos~~, Y.S]]	+	[[Category: Schutter, J W.De]]
		+	[[Category: Transferase-transferase inhibitor complex]]

OCA at 14:12, 24 December 2014

OCA — Wed, 24 Dec 2014 14:12:17 GMT

←Older revision		Revision as of 14:12, 24 December 2014
Line 6:		Line 6:

	Description: Crystal structure of human FPPS in complex with nickel, JDS05120, and sulfate		Description: Crystal structure of human FPPS in complex with nickel, JDS05120, and sulfate
		+	[[Category: Unreleased Structures]]
		+	[[Category: De Schutter, J.W]]
		+	[[Category: Park, J]]
		+	[[Category: Berghuis, A.M]]
		+	[[Category: Tsantrizos, Y.S]]

OCA at 07:34, 7 May 2014

OCA — Wed, 07 May 2014 07:34:08 GMT

←Older revision		Revision as of 07:34, 7 May 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Park, J., De schutter, J.W., Tsantrizos, Y.S., Berghuis, A.M.		Authors: Park, J., De schutter, J.W., Tsantrizos, Y.S., Berghuis, A.M.

	Description: Crystal structure of human FPPS in complex with nickel, JDS05120, and sulfate		Description: Crystal structure of human FPPS in complex with nickel, JDS05120, and sulfate

OCA at 06:44, 22 January 2014

OCA — Wed, 22 Jan 2014 06:44:03 GMT

←Older revision		Revision as of 06:44, 22 January 2014
Line 3:		Line 3:
	The entry 4nfk is ON HOLD		The entry 4nfk is ON HOLD

-	Authors: Park, J., De ~~Schutter~~, J.W., Tsantrizos, Y.S., Berghuis, A.M.	+	Authors: Park, J., De schutter, J.W., Tsantrizos, Y.S., Berghuis, A.M.

	Description: Crystal structure of human FPPS in complex with nickel, JDS05120, and sulfate		Description: Crystal structure of human FPPS in complex with nickel, JDS05120, and sulfate

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

OCA — Wed, 13 Nov 2013 07:46:54 GMT

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

←Older revision

Revision as of 07:46, 13 November 2013