5nwo - Revision history

OCA: Redirecting to 6y3e

2020-03-04T06:36:59Z

Redirecting to 6y3e

←Older revision		Revision as of 06:36, 4 March 2020
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-		+	#REDIRECT [[6y3e]] This PDB entry is obsolete and replaced by 6y3e
-	~~==Scaffold-ligand complex==~~	+
-	~~<StructureSection load='5nwo' size='340' side='right'caption='~~[[~~5nwo]], [[Resolution\|resolution]] 1.45Å' scene=''>~~	+
-	~~== Structural highlights ==~~	+
-	~~<table><tr><td colspan='2'>[[5nwo~~]] is a 1 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=5NWO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NWO FirstGlance]. <br>	+
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=12P:DODECAETHYLENE+GLYCOL'>12P</scene>, <scene name='pdbligand=9CK:1-[(4-aminophenyl)methyl]-3-[2-[2-(2-bromophenyl)pyrazolidin-1-yl]-2-oxidanylidene-ethyl]urea'>9CK</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>	+
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PPIF, CYP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=5nwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nwo OCA], [http://pdbe.org/5nwo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nwo RCSB], [http://www.ebi.ac.uk/pdbsum/5nwo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nwo ProSAT]</span></td></tr>	+
-	~~</table>~~	+
-	~~== Function ==~~	+
-	[[http://www.uniprot.org/uniprot/PPIF_HUMAN PPIF_HUMAN]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probablity of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress-induced necrosis. Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels. Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis.<ref>PMID:19228691</ref> <ref>PMID:22726440</ref>	+
-		+
-	~~==See Also==~~	+
-	*[[Cyclophilin 3D structures\|Cyclophilin 3D structures]]	+
-	~~== References ==~~	+
-	~~<references/>~~	+
-	~~__TOC__~~	+
-	~~</StructureSection>~~	+
-	~~[[Category: Human]]~~	+
-	~~[[Category: Large Structures]]~~	+
-	~~[[Category: Peptidylprolyl isomerase]]~~	+
-	~~[[Category: Lian, L Y]]~~	+
-	~~[[Category: Zacharchenko, T]]~~	+
-	~~[[Category: Isomerase]]~~	+
-	~~[[Category: Mitochondrial]]~~	+
-	~~[[Category: Peptidyl-prolyl cis-trans isomerase f]]~~	+

OCA at 11:23, 13 November 2019

2019-11-13T11:23:22Z

←Older revision		Revision as of 11:23, 13 November 2019
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-	==~~Human Cyclophilin D Complexed with Inhibitor~~==	+	==Scaffold-ligand complex==
-	<StructureSection load='5nwo' size='340' side='right' caption='[[5nwo]], [[Resolution\|resolution]] 1.45Å' scene=''>	+	<StructureSection load='5nwo' size='340' side='right'caption='[[5nwo]], [[Resolution\|resolution]] 1.45Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5nwo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NWO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NWO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5nwo]] is a 1 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=5NWO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NWO FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=12P:DODECAETHYLENE+GLYCOL'>12P</scene>, <scene name='pdbligand=9CK:1-[(4-aminophenyl)methyl]-3-[2-[2-(2-bromophenyl)pyrazolidin-1-yl]-2-oxidanylidene-ethyl]urea'>9CK</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=12P:DODECAETHYLENE+GLYCOL'>12P</scene>, <scene name='pdbligand=9CK:1-[(4-aminophenyl)methyl]-3-[2-[2-(2-bromophenyl)pyrazolidin-1-yl]-2-oxidanylidene-ethyl]urea'>9CK</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PPIF, CYP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=5nwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nwo OCA], [http://pdbe.org/5nwo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nwo RCSB], [http://www.ebi.ac.uk/pdbsum/5nwo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nwo 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=5nwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nwo OCA], [http://pdbe.org/5nwo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nwo RCSB], [http://www.ebi.ac.uk/pdbsum/5nwo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nwo ProSAT]</span></td></tr>
Line 10:		Line 11:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/PPIF_HUMAN PPIF_HUMAN]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probablity of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress-induced necrosis. Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels. Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis.<ref>PMID:19228691</ref> <ref>PMID:22726440</ref>		[[http://www.uniprot.org/uniprot/PPIF_HUMAN PPIF_HUMAN]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probablity of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress-induced necrosis. Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels. Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis.<ref>PMID:19228691</ref> <ref>PMID:22726440</ref>
		+
		+	==See Also==
		+	*[[Cyclophilin 3D structures\|Cyclophilin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
	[[Category: Lian, L Y]]		[[Category: Lian, L Y]]

OCA at 05:25, 30 May 2018

2018-05-30T05:25:13Z

←Older revision		Revision as of 05:25, 30 May 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5nwo is ~~ON HOLD until Paper Publication~~	+	==Human Cyclophilin D Complexed with Inhibitor==
-		+	<StructureSection load='5nwo' size='340' side='right' caption='[[5nwo]], [[Resolution\|resolution]] 1.45Å' scene=''>
-	~~Authors~~: ~~Zacharchenko~~, T., ~~Lian~~, L.Y.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5nwo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NWO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NWO FirstGlance]. <br>
-	~~Description~~: ~~Human Cyclophilin D Complexed~~ with ~~Inhibitor~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=12P:DODECAETHYLENE+GLYCOL'>12P</scene>, <scene name='pdbligand=9CK:1-[(4-aminophenyl)methyl]-3-[2-[2-(2-bromophenyl)pyrazolidin-1-yl]-2-oxidanylidene-ethyl]urea'>9CK</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=5nwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nwo OCA], [http://pdbe.org/5nwo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nwo RCSB], [http://www.ebi.ac.uk/pdbsum/5nwo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nwo ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PPIF_HUMAN PPIF_HUMAN]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probablity of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress-induced necrosis. Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels. Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis.<ref>PMID:19228691</ref> <ref>PMID:22726440</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Peptidylprolyl isomerase]]
		+	[[Category: Lian, L Y]]
	[[Category: Zacharchenko, T]]		[[Category: Zacharchenko, T]]
-	[[Category: ~~Lian, L.Y~~]]	+	[[Category: Isomerase]]
		+	[[Category: Mitochondrial]]
		+	[[Category: Peptidyl-prolyl cis-trans isomerase f]]

OCA: Protected "5nwo" [edit=sysop:move=sysop]

2017-05-17T12:21:44Z

Protected "5nwo" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:21, 17 May 2017

OCA: New page: '''Unreleased structure''' The entry 5nwo is ON HOLD until Paper Publication Authors: Zacharchenko, T., Lian, L.Y. Description: Human Cyclophilin D Complexed with Inhibitor [[Category:...

2017-05-17T12:21:42Z

New page: '''Unreleased structure''' The entry 5nwo is ON HOLD until Paper Publication Authors: Zacharchenko, T., Lian, L.Y. Description: Human Cyclophilin D Complexed with Inhibitor [[Category:...

New page

'''Unreleased structure'''

The entry 5nwo is ON HOLD until Paper Publication

Authors: Zacharchenko, T., Lian, L.Y.

Description: Human Cyclophilin D Complexed with Inhibitor
[[Category: Unreleased Structures]]
[[Category: Zacharchenko, T]]
[[Category: Lian, L.Y]]