4d4z - Revision history

OCA at 11:17, 9 May 2024

OCA — Thu, 09 May 2024 11:17:43 GMT

←Older revision		Revision as of 11:17, 9 May 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4d4z]] is a 2 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=4D4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D4Z FirstGlance]. <br>		<table><tr><td colspan='2'>[[4d4z]] is a 2 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=4D4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D4Z FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B3P:2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>B3P</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</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]] 1.7Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B3P:2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>B3P</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</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=4d4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d4z OCA], [https://pdbe.org/4d4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d4z RCSB], [https://www.ebi.ac.uk/pdbsum/4d4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d4z 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=4d4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d4z OCA], [https://pdbe.org/4d4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d4z RCSB], [https://www.ebi.ac.uk/pdbsum/4d4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d4z ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/DOHH_HUMAN DOHH_HUMAN]] Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.[HAMAP-Rule:MF_03101]<ref>PMID:16371467</ref> <ref>PMID:19706422</ref>	+	[https://www.uniprot.org/uniprot/DOHH_HUMAN DOHH_HUMAN] Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.[HAMAP-Rule:MF_03101]<ref>PMID:16371467</ref> <ref>PMID:19706422</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 07:47, 14 September 2022

OCA — Wed, 14 Sep 2022 07:47:39 GMT

←Older revision		Revision as of 07:47, 14 September 2022
Line 3:		Line 3:
	<StructureSection load='4d4z' size='340' side='right'caption='[[4d4z]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='4d4z' size='340' side='right'caption='[[4d4z]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4d4z]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D4Z OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4D4Z FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4d4z]] is a 2 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=4D4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D4Z FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B3P:2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>B3P</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B3P:2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>B3P</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4d50\|4d50]]</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=4d4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d4z OCA], [https://pdbe.org/4d4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d4z RCSB], [https://www.ebi.ac.uk/pdbsum/4d4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d4z 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/Deoxyhypusine_monooxygenase Deoxyhypusine monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.29 1.14.99.29] </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=4d4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d4z OCA], [~~http~~://pdbe.org/4d4z PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4d4z RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4d4z PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4d4z ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/DOHH_HUMAN DOHH_HUMAN]] Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.[HAMAP-Rule:MF_03101]<ref>PMID:16371467</ref> <ref>PMID:19706422</ref>	+	[[https://www.uniprot.org/uniprot/DOHH_HUMAN DOHH_HUMAN]] Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.[HAMAP-Rule:MF_03101]<ref>PMID:16371467</ref> <ref>PMID:19706422</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Deoxyhypusine monooxygenase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Han, Z]]	+	[[Category: Han Z]]
-	[[Category: Hilgenfeld, R]]	+	[[Category: Hilgenfeld R]]
-	[[Category: Sakai, N]]	+	[[Category: Sakai N]]
-	~~[[Category: Eif-5a]]~~	+
-	~~[[Category: Hypusine]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 08:10, 27 March 2019

OCA — Wed, 27 Mar 2019 08:10:46 GMT

←Older revision		Revision as of 08:10, 27 March 2019
Line 1:		Line 1:

	==STRUCTURE OF HUMAN DEOXYHYPUSINE HYDROXYLASE in complex with glycerol==		==STRUCTURE OF HUMAN DEOXYHYPUSINE HYDROXYLASE in complex with glycerol==
-	<StructureSection load='4d4z' size='340' side='right' caption='[[4d4z]], [[Resolution\|resolution]] 1.70Å' scene=''>	+	<StructureSection load='4d4z' size='340' side='right'caption='[[4d4z]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4d4z]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D4Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D4Z FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4d4z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D4Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D4Z FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B3P:2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>B3P</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B3P:2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>B3P</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4d50\|4d50]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4d50\|4d50]]</td></tr>
Line 25:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Deoxyhypusine monooxygenase]]		[[Category: Deoxyhypusine monooxygenase]]
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Han, Z]]		[[Category: Han, Z]]
	[[Category: Hilgenfeld, R]]		[[Category: Hilgenfeld, R]]

OCA at 17:30, 9 March 2017

OCA — Thu, 09 Mar 2017 17:30:10 GMT

←Older revision		Revision as of 17:30, 9 March 2017
Line 1:		Line 1:
		+
	==STRUCTURE OF HUMAN DEOXYHYPUSINE HYDROXYLASE in complex with glycerol==		==STRUCTURE OF HUMAN DEOXYHYPUSINE HYDROXYLASE in complex with glycerol==
	<StructureSection load='4d4z' size='340' side='right' caption='[[4d4z]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='4d4z' size='340' side='right' caption='[[4d4z]], [[Resolution\|resolution]] 1.70Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4d50\|4d50]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4d50\|4d50]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Deoxyhypusine_monooxygenase Deoxyhypusine monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.29 1.14.99.29] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Deoxyhypusine_monooxygenase Deoxyhypusine monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.29 1.14.99.29] </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=4d4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d4z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d4z RCSB], [http://www.ebi.ac.uk/pdbsum/4d4z 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=4d4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d4z OCA], [http://pdbe.org/4d4z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d4z RCSB], [http://www.ebi.ac.uk/pdbsum/4d4z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d4z 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 4d4z" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:00, 22 April 2015

OCA — Wed, 22 Apr 2015 07:00:36 GMT

←Older revision		Revision as of 07:00, 22 April 2015
Line 10:		Line 10:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/DOHH_HUMAN DOHH_HUMAN]] Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.[HAMAP-Rule:MF_03101]<ref>PMID:16371467</ref> <ref>PMID:19706422</ref>		[[http://www.uniprot.org/uniprot/DOHH_HUMAN DOHH_HUMAN]] Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.[HAMAP-Rule:MF_03101]<ref>PMID:16371467</ref> <ref>PMID:19706422</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Deoxyhypusine hydroxylase (DOHH) is a non-heme diiron enzyme involved in the posttranslational modification of a critical lysine residue of eukaryotic translation initiation factor 5A (eIF-5A) to yield the unusual amino acid residue hypusine. This modification is essential for the role of eIF-5A in translation and in nuclear export of a group of specific mRNAs. The diiron center of human DOHH (hDOHH) forms a peroxo-diiron(III) intermediate (hDOHHperoxo) when its reduced form reacts with O2. hDOHHperoxo has a lifetime exceeding that of the peroxo intermediates of other diiron enzymes by several orders of magnitude. Here we report the 1.7-A crystal structures of hDOHHperoxo and a complex with glycerol. The structure of hDOHHperoxo reveals the presence of a mu-1,2-peroxo-diiron(III) species at the active site. Augmented by UV/Vis and Mossbauer spectroscopic studies, the crystal structures offer explanations for the extreme longevity of hDOHHperoxo and illustrate how the enzyme specifically recognizes its only substrate, deoxyhypusine-eIF-5A.
		+
		+	Crystal Structure of the Peroxo-diiron(III) Intermediate of Deoxyhypusine Hydroxylase, an Oxygenase Involved in Hypusination.,Han Z, Sakai N, Bottger LH, Klinke S, Hauber J, Trautwein AX, Hilgenfeld R Structure. 2015 Apr 9. pii: S0969-2126(15)00080-5. doi:, 10.1016/j.str.2015.03.002. PMID:25865244<ref>PMID:25865244</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:57, 15 April 2015

OCA — Wed, 15 Apr 2015 12:57:02 GMT

←Older revision		Revision as of 12:57, 15 April 2015
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==STRUCTURE OF HUMAN DEOXYHYPUSINE HYDROXYLASE in complex with glycerol==
-		+	<StructureSection load='4d4z' size='340' side='right' caption='[[4d4z]], [[Resolution\|resolution]] 1.70Å' scene=''>
-	~~The entry~~ 4d4z is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4d4z]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D4Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D4Z FirstGlance]. <br>
-	~~Authors~~: ~~HAN~~, Z., ~~SAKAI~~, N., ~~HILGENFELD, R~~.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B3P:2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>B3P</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene></td></tr>
-		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4d50\|4d50]]</td></tr>
-	~~Description: STRUCTURE OF HUMAN DEOXYHYPUSINE HYDROXYLASE in complex with glycerol~~	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Deoxyhypusine_monooxygenase Deoxyhypusine monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.29 1.14.99.29] </span></td></tr>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	<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=4d4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d4z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d4z RCSB], [http://www.ebi.ac.uk/pdbsum/4d4z PDBsum]</span></td></tr>
-	[[Category: ~~Hilgenfeld, R~~]]	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DOHH_HUMAN DOHH_HUMAN]] Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.[HAMAP-Rule:MF_03101]<ref>PMID:16371467</ref> <ref>PMID:19706422</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Deoxyhypusine monooxygenase]]
	[[Category: Han, Z]]		[[Category: Han, Z]]
		+	[[Category: Hilgenfeld, R]]
	[[Category: Sakai, N]]		[[Category: Sakai, N]]
		+	[[Category: Eif-5a]]
		+	[[Category: Hypusine]]
		+	[[Category: Oxidoreductase]]

OCA at 06:22, 8 April 2015

OCA — Wed, 08 Apr 2015 06:22:44 GMT

←Older revision		Revision as of 06:22, 8 April 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4d4z is ON HOLD	+	The entry 4d4z is ON HOLD until Paper Publication

	Authors: HAN, Z., SAKAI, N., HILGENFELD, R.		Authors: HAN, Z., SAKAI, N., HILGENFELD, R.

OCA at 13:48, 24 December 2014

OCA — Wed, 24 Dec 2014 13:48:57 GMT

←Older revision		Revision as of 13:48, 24 December 2014
Line 6:		Line 6:

	Description: STRUCTURE OF HUMAN DEOXYHYPUSINE HYDROXYLASE in complex with glycerol		Description: STRUCTURE OF HUMAN DEOXYHYPUSINE HYDROXYLASE in complex with glycerol
		+	[[Category: Unreleased Structures]]
		+	[[Category: Hilgenfeld, R]]
		+	[[Category: Han, Z]]
		+	[[Category: Sakai, N]]

OCA: Protected "4d4z" [edit=sysop:move=sysop]

OCA — Wed, 19 Nov 2014 11:06:46 GMT

Protected "4d4z" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:06, 19 November 2014

OCA: New page: '''Unreleased structure''' The entry 4d4z is ON HOLD Authors: HAN, Z., SAKAI, N., HILGENFELD, R. Description: STRUCTURE OF HUMAN DEOXYHYPUSINE HYDROXYLASE in complex with glycerol

OCA — Wed, 19 Nov 2014 11:06:45 GMT

New page: '''Unreleased structure''' The entry 4d4z is ON HOLD Authors: HAN, Z., SAKAI, N., HILGENFELD, R. Description: STRUCTURE OF HUMAN DEOXYHYPUSINE HYDROXYLASE in complex with glycerol

New page

'''Unreleased structure'''

The entry 4d4z is ON HOLD

Authors: HAN, Z., SAKAI, N., HILGENFELD, R.

Description: STRUCTURE OF HUMAN DEOXYHYPUSINE HYDROXYLASE in complex with glycerol