4qpd - Revision history

OCA at 08:59, 20 March 2024

OCA — Wed, 20 Mar 2024 08:59:11 GMT

←Older revision		Revision as of 08:59, 20 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4qpd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QPD FirstGlance]. <br>		<table><tr><td colspan='2'>[[4qpd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QPD FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</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]] 2.1Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</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=4qpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qpd OCA], [https://pdbe.org/4qpd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qpd RCSB], [https://www.ebi.ac.uk/pdbsum/4qpd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qpd 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=4qpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qpd OCA], [https://pdbe.org/4qpd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qpd RCSB], [https://www.ebi.ac.uk/pdbsum/4qpd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qpd ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/E3NZ06_DANRE E3NZ06_DANRE]		[https://www.uniprot.org/uniprot/E3NZ06_DANRE E3NZ06_DANRE]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	10-Formyltetrahydrofolate dehydrogenase (FDH), which is composed of a small N-terminal domain (Nt-FDH) and a large C-terminal domain, is an abundant folate enzyme in the liver and converts 10-formyltetrahydrofolate (10-FTHF) to tetrahydrofolate (THF) and CO2. Nt-FDH alone possesses a hydrolase activity, which converts 10-FTHF to THF and formate in the presence of beta-mercaptoethanol. To elucidate the catalytic mechanism of Nt-FDH, crystal structures of apo-form zNt-FDH from zebrafish and its complexes with the substrate analogue 10-formyl-5,8-dideazafolate (10-FDDF) and with the products THF and formate have been determined. The structures reveal that the conformations of three loops (residues 86-90, 135-143 and 200-203) are altered upon ligand (10-FDDF or THF) binding in the active site. The orientations and geometries of key residues, including Phe89, His106, Arg114, Asp142 and Tyr200, are adjusted for substrate binding and product release during catalysis. Among them, Tyr200 is especially crucial for product release. An additional potential THF binding site is identified in the cavity between two zNt-FDH molecules, which might contribute to the properties of product inhibition and THF storage reported for FDH. Together with mutagenesis studies and activity assays, the structures of zNt-FDH and its complexes provide a coherent picture of the active site and a potential THF binding site of zNt-FDH along with the substrate and product specificity, lending new insights into the molecular mechanism underlying the enzymatic properties of Nt-FDH.
-
-	Structures of the hydrolase domain of zebrafish 10-formyltetrahydrofolate dehydrogenase and its complexes reveal a complete set of key residues for hydrolysis and product inhibition.,Lin CC, Chuankhayan P, Chang WN, Kao TT, Guan HH, Fun HK, Nakagawa A, Fu TF, Chen CJ Acta Crystallogr D Biol Crystallogr. 2015 Apr;71(Pt 4):1006-21. doi:, 10.1107/S1399004715002928. Epub 2015 Mar 27. PMID:25849409<ref>PMID:25849409</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4qpd" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 13:45, 22 February 2023

OCA — Wed, 22 Feb 2023 13:45:05 GMT

←Older revision		Revision as of 13:45, 22 February 2023
Line 3:		Line 3:
	<StructureSection load='4qpd' size='340' side='right'caption='[[4qpd]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='4qpd' size='340' side='right'caption='[[4qpd]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4qpd]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Brachidanio_rerio Brachidanio~~ rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QPD OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4QPD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4qpd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QPD FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ts4\|4ts4]], [[4tt8\|4tt8]], [[4tts\|4tts]], [[4qpc\|4qpc]], [[4r8v\|4r8v]]</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=4qpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qpd OCA], [https://pdbe.org/4qpd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qpd RCSB], [https://www.ebi.ac.uk/pdbsum/4qpd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qpd ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">aldh1l1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7955 Brachidanio rerio])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Formyltetrahydrofolate_dehydrogenase Formyltetrahydrofolate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.6 1.5.1.6] </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=4qpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qpd OCA], [~~http~~://pdbe.org/4qpd PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4qpd RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4qpd PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4qpd ProSAT]</span></td></tr>	+
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/E3NZ06_DANRE E3NZ06_DANRE]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Brachidanio~~ rerio]]	+	[[Category: Danio rerio]]
-	~~[[Category: Formyltetrahydrofolate dehydrogenase~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Chang~~, W N~~]]	+	[[Category: Chang WN]]
-	[[Category: Chen~~, C J~~]]	+	[[Category: Chen CJ]]
-	[[Category: Chuankhayan, P]]	+	[[Category: Chuankhayan P]]
-	[[Category: Fu~~, T F~~]]	+	[[Category: Fu TF]]
-	[[Category: Kao~~, T T~~]]	+	[[Category: Kao TT]]
-	[[Category: Lin~~, C C]]~~	+	[[Category: Lin CC]]
-	~~[[Category: 10-formyltetrahydrofolate dehydrogenase]]~~	+
-	~~[[Category: Catalysis]]~~	+
-	~~[[Category: Hydrolase domain]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 08:23, 18 December 2019

OCA — Wed, 18 Dec 2019 08:23:08 GMT

←Older revision		Revision as of 08:23, 18 December 2019
Line 10:		Line 10:
	<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=4qpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qpd OCA], [http://pdbe.org/4qpd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qpd RCSB], [http://www.ebi.ac.uk/pdbsum/4qpd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qpd 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=4qpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qpd OCA], [http://pdbe.org/4qpd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qpd RCSB], [http://www.ebi.ac.uk/pdbsum/4qpd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qpd ProSAT]</span></td></tr>
	</table>		</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	10-Formyltetrahydrofolate dehydrogenase (FDH), which is composed of a small N-terminal domain (Nt-FDH) and a large C-terminal domain, is an abundant folate enzyme in the liver and converts 10-formyltetrahydrofolate (10-FTHF) to tetrahydrofolate (THF) and CO2. Nt-FDH alone possesses a hydrolase activity, which converts 10-FTHF to THF and formate in the presence of beta-mercaptoethanol. To elucidate the catalytic mechanism of Nt-FDH, crystal structures of apo-form zNt-FDH from zebrafish and its complexes with the substrate analogue 10-formyl-5,8-dideazafolate (10-FDDF) and with the products THF and formate have been determined. The structures reveal that the conformations of three loops (residues 86-90, 135-143 and 200-203) are altered upon ligand (10-FDDF or THF) binding in the active site. The orientations and geometries of key residues, including Phe89, His106, Arg114, Asp142 and Tyr200, are adjusted for substrate binding and product release during catalysis. Among them, Tyr200 is especially crucial for product release. An additional potential THF binding site is identified in the cavity between two zNt-FDH molecules, which might contribute to the properties of product inhibition and THF storage reported for FDH. Together with mutagenesis studies and activity assays, the structures of zNt-FDH and its complexes provide a coherent picture of the active site and a potential THF binding site of zNt-FDH along with the substrate and product specificity, lending new insights into the molecular mechanism underlying the enzymatic properties of Nt-FDH.
		+
		+	Structures of the hydrolase domain of zebrafish 10-formyltetrahydrofolate dehydrogenase and its complexes reveal a complete set of key residues for hydrolysis and product inhibition.,Lin CC, Chuankhayan P, Chang WN, Kao TT, Guan HH, Fun HK, Nakagawa A, Fu TF, Chen CJ Acta Crystallogr D Biol Crystallogr. 2015 Apr;71(Pt 4):1006-21. doi:, 10.1107/S1399004715002928. Epub 2015 Mar 27. PMID:25849409<ref>PMID:25849409</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4qpd" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 08:49, 24 April 2019

OCA — Wed, 24 Apr 2019 08:49:43 GMT

←Older revision		Revision as of 08:49, 24 April 2019
Line 1:		Line 1:

	==Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase (wild-type) complex with tetrahydrofolate==		==Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase (wild-type) complex with tetrahydrofolate==
-	<StructureSection load='4qpd' size='340' side='right' caption='[[4qpd]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='4qpd' size='340' side='right'caption='[[4qpd]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4qpd]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QPD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QPD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4qpd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Brachidanio_rerio Brachidanio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QPD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QPD FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ts4\|4ts4]], [[4tt8\|4tt8]], [[4tts\|4tts]], [[4qpc\|4qpc]], [[4r8v\|4r8v]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ts4\|4ts4]], [[4tt8\|4tt8]], [[4tts\|4tts]], [[4qpc\|4qpc]], [[4r8v\|4r8v]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">aldh1l1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7955 Brachidanio rerio])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Formyltetrahydrofolate_dehydrogenase Formyltetrahydrofolate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.6 1.5.1.6] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Formyltetrahydrofolate_dehydrogenase Formyltetrahydrofolate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.6 1.5.1.6] </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=4qpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qpd OCA], [http://pdbe.org/4qpd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qpd RCSB], [http://www.ebi.ac.uk/pdbsum/4qpd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qpd 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=4qpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qpd OCA], [http://pdbe.org/4qpd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qpd RCSB], [http://www.ebi.ac.uk/pdbsum/4qpd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qpd ProSAT]</span></td></tr>
Line 11:		Line 12:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Brachidanio rerio]]
	[[Category: Formyltetrahydrofolate dehydrogenase]]		[[Category: Formyltetrahydrofolate dehydrogenase]]
		+	[[Category: Large Structures]]
	[[Category: Chang, W N]]		[[Category: Chang, W N]]
	[[Category: Chen, C J]]		[[Category: Chen, C J]]

OCA at 17:24, 18 January 2017

OCA — Wed, 18 Jan 2017 17:24:38 GMT

←Older revision		Revision as of 17:24, 18 January 2017
Line 1:		Line 1:
		+
	==Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase (wild-type) complex with tetrahydrofolate==		==Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase (wild-type) complex with tetrahydrofolate==
	<StructureSection load='4qpd' size='340' side='right' caption='[[4qpd]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='4qpd' size='340' side='right' caption='[[4qpd]], [[Resolution\|resolution]] 2.10Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ts4\|4ts4]], [[4tt8\|4tt8]], [[4tts\|4tts]], [[4qpc\|4qpc]], [[4r8v\|4r8v]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ts4\|4ts4]], [[4tt8\|4tt8]], [[4tts\|4tts]], [[4qpc\|4qpc]], [[4r8v\|4r8v]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Formyltetrahydrofolate_dehydrogenase Formyltetrahydrofolate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.6 1.5.1.6] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Formyltetrahydrofolate_dehydrogenase Formyltetrahydrofolate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.6 1.5.1.6] </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=4qpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qpd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qpd RCSB], [http://www.ebi.ac.uk/pdbsum/4qpd 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=4qpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qpd OCA], [http://pdbe.org/4qpd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qpd RCSB], [http://www.ebi.ac.uk/pdbsum/4qpd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qpd ProSAT]</span></td></tr>
	</table>		</table>
	__TOC__		__TOC__

OCA at 12:59, 15 April 2015

OCA — Wed, 15 Apr 2015 12:59:21 GMT

←Older revision		Revision as of 12:59, 15 April 2015
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase (wild-type) complex with tetrahydrofolate==
-		+	<StructureSection load='4qpd' size='340' side='right' caption='[[4qpd]], [[Resolution\|resolution]] 2.10Å' scene=''>
-	~~The entry~~ 4qpd is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4qpd]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QPD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QPD FirstGlance]. <br>
-	~~Authors~~: ~~Lin, C~~.C.~~, Chen, C~~.J.~~, Fu, T~~.F.~~, Chuankhayan, P~~.~~, Kao, T~~.~~T., Chang, W.N~~.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</scene></td></tr>
-		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ts4\|4ts4]], [[4tt8\|4tt8]], [[4tts\|4tts]], [[4qpc\|4qpc]], [[4r8v\|4r8v]]</td></tr>
-	~~Description~~: ~~Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase~~ (~~wild-type~~) ~~complex with tetrahydrofolate~~	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Formyltetrahydrofolate_dehydrogenase Formyltetrahydrofolate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.6 1.5.1.6] </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=4qpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qpd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qpd RCSB], [http://www.ebi.ac.uk/pdbsum/4qpd PDBsum]</span></td></tr>
-	[[~~Category~~: ~~Chang~~, W.N]]	+	</table>
-	[[~~Category~~: Fu, T.F]]	+	__TOC__
-	[[Category: ~~Lin, C.C~~]]	+	</StructureSection>
-	[[Category: ~~Kao~~, ~~T.T~~]]	+	[[Category: Formyltetrahydrofolate dehydrogenase]]
-	[[Category: Chen, C.J]]	+	[[Category: Chang, W N]]
		+	[[Category: Chen, C J]]
	[[Category: Chuankhayan, P]]		[[Category: Chuankhayan, P]]
		+	[[Category: Fu, T F]]
		+	[[Category: Kao, T T]]
		+	[[Category: Lin, C C]]
		+	[[Category: 10-formyltetrahydrofolate dehydrogenase]]
		+	[[Category: Catalysis]]
		+	[[Category: Hydrolase domain]]
		+	[[Category: Oxidoreductase]]

OCA at 16:00, 24 December 2014

OCA — Wed, 24 Dec 2014 16:00:41 GMT

←Older revision		Revision as of 16:00, 24 December 2014
Line 6:		Line 6:

	Description: Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase (wild-type) complex with tetrahydrofolate		Description: Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase (wild-type) complex with tetrahydrofolate
		+	[[Category: Unreleased Structures]]
		+	[[Category: Chang, W.N]]
		+	[[Category: Fu, T.F]]
		+	[[Category: Lin, C.C]]
		+	[[Category: Kao, T.T]]
		+	[[Category: Chen, C.J]]
		+	[[Category: Chuankhayan, P]]

OCA at 09:47, 16 July 2014

OCA — Wed, 16 Jul 2014 09:47:15 GMT

←Older revision		Revision as of 09:47, 16 July 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Lin, C.C., Chen, C.J., Fu, T.F., Chuankhayan, P., Kao, T.T., Chang, W.N.		Authors: Lin, C.C., Chen, C.J., Fu, T.F., Chuankhayan, P., Kao, T.T., Chang, W.N.

	Description: Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase (wild-type) complex with tetrahydrofolate		Description: Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase (wild-type) complex with tetrahydrofolate

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

OCA — Wed, 02 Jul 2014 07:27:28 GMT

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

←Older revision

Revision as of 07:27, 2 July 2014

OCA: New page: '''Unreleased structure''' The entry 4qpd is ON HOLD Authors: Lin, C.C., Chen, C.J., Fu, T.F., Chuankhayan, P., Kao, T.T., Chang, W.N. Description: Crystal structure of the hydrolase d...

OCA — Wed, 02 Jul 2014 07:27:27 GMT

New page: '''Unreleased structure''' The entry 4qpd is ON HOLD Authors: Lin, C.C., Chen, C.J., Fu, T.F., Chuankhayan, P., Kao, T.T., Chang, W.N. Description: Crystal structure of the hydrolase d...

New page

'''Unreleased structure'''

The entry 4qpd is ON HOLD

Authors: Lin, C.C., Chen, C.J., Fu, T.F., Chuankhayan, P., Kao, T.T., Chang, W.N.

Description: Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase (wild-type) complex with tetrahydrofolate