1fq6 - Revision history

OCA at 11:15, 27 March 2024

OCA — Wed, 27 Mar 2024 11:15:35 GMT

←Older revision		Revision as of 11:15, 27 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1fq6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FQ6 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1fq6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FQ6 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0QF:N-[(1R)-2-{[(1R,2R,3S)-1-(CYCLOHEXYLMETHYL)-2,3-DIHYDROXY-5-METHYLHEXYL]AMINO}-1-(ETHYLSULFANYL)-2-OXOETHYL]-NALPHA-(MORPHOLIN-4-YLSULFONYL)-D-PHENYLALANINAMIDE'>0QF</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=~~NAG~~:N-~~ACETYL~~-~~D-GLUCOSAMINE~~'>~~NAG~~</scene>, <scene name='pdbligand=~~GUP~~:~~ALPHA~~-L-~~GULOPYRANOSIDE~~'>~~GUP~~</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]] 2.7Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2jxr\|2jxr]], [[1dp5\|1dp5]], [[1fq4\|1fq4]], [[1fq5\|1fq5]], [[1fq7\|1fq7]], [[1fq8\|1fq8]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0QF:N-[(1R)-2-{[(1R,2R,3S)-1-(CYCLOHEXYLMETHYL)-2,3-DIHYDROXY-5-METHYLHEXYL]AMINO}-1-(ETHYLSULFANYL)-2-OXOETHYL]-NALPHA-(MORPHOLIN-4-YLSULFONYL)-D-PHENYLALANINAMIDE'>0QF</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GUP:ALPHA-L-GULOPYRANOSIDE'>GUP</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Saccharopepsin Saccharopepsin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.25 3.4.23.25] </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=1fq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fq6 OCA], [https://pdbe.org/1fq6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fq6 RCSB], [https://www.ebi.ac.uk/pdbsum/1fq6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fq6 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=1fq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fq6 OCA], [https://pdbe.org/1fq6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fq6 RCSB], [https://www.ebi.ac.uk/pdbsum/1fq6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fq6 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CARP_YEAST CARP_YEAST]] Aspartyl protease implicated in the post-translational regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY and on itself.	+	[https://www.uniprot.org/uniprot/CARP_YEAST CARP_YEAST] Aspartyl protease implicated in the post-translational regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY and on itself.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 21:		Line 20:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fq6 ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fq6 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Saccharopepsin is a vacuolar aspartic proteinase involved in activation of a number of hydrolases. The enzyme has great structural homology to mammalian aspartic proteinases including human renin and we have used it as a model system to study the binding of renin inhibitors by X-ray crystallography. Five medium-to-high resolution structures of saccharopepsin complexed with transition-state analogue renin inhibitors were determined. The structure of a cyclic peptide inhibitor (PD-129,541) complexed with the proteinase was solved to 2.5 A resolution. This inhibitor has low affinity for human renin yet binds very tightly to the yeast proteinase (K(i)=4 nM). The high affinity of this inhibitor can be attributed to its bulky cyclic moiety spanning P(2)-P(3)' and other residues that appear to optimally fit the binding sub-sites of the enzyme. Superposition of the saccharopepsin structure on that of renin showed that a movement of the loop 286-301 relative to renin facilitates tighter binding of this inhibitor to saccharopepsin. Our 2.8 A resolution structure of the complex with CP-108,420 shows that its benzimidazole P(3 )replacement retains one of the standard hydrogen bonds that normally involve the inhibitor's main-chain. This suggests a non-peptide lead in overcoming the problem of susceptible peptide bonds in the design of aspartic proteinase inhibitors. CP-72,647 which possesses a basic histidine residue at P(2), has a high affinity for renin (K(i)=5 nM) but proves to be a poor inhibitor for saccharopepsin (K(i)=3.7 microM). This may stem from the fact that the histidine residue would not bind favourably with the predominantly hydrophobic S(2) sub-site of saccharopepsin.
-
-	X-ray structures of five renin inhibitors bound to saccharopepsin: exploration of active-site specificity.,Cronin NB, Badasso MO, J Tickle I, Dreyer T, Hoover DJ, Rosati RL, Humblet CC, Lunney EA, Cooper JB J Mol Biol. 2000 Nov 10;303(5):745-60. PMID:11061973<ref>PMID:11061973</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1fq6" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Pepsin\|Pepsin]]		*[[Pepsin\|Pepsin]]
	*[[Proteinase 3D structures\|Proteinase 3D structures]]		*[[Proteinase 3D structures\|Proteinase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]
-	~~[[Category: Saccharopepsin]]~~	+	[[Category: Badasso MO]]
-	[[Category: Badasso~~, M O~~]]	+	[[Category: Cooper JB]]
-	[[Category: Cooper~~, J B~~]]	+	[[Category: Cronin NB]]
-	[[Category: Cronin~~, N B~~]]	+	[[Category: Dreyer T]]
-	[[Category: Dreyer, T]]	+	[[Category: Hoover DJ]]
-	[[Category: Hoover~~, D J~~]]	+	[[Category: Humblet CC]]
-	[[Category: Humblet~~, C C~~]]	+	[[Category: Lunney EA]]
-	[[Category: Lunney~~, E A~~]]	+	[[Category: Rosati RL]]
-	[[Category: Rosati~~, R L~~]]	+	[[Category: Tickle IJ]]
-	[[Category: Tickle~~, I J]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Hydrolase-hydrolase inhibitor complex~~]]	+

OCA at 07:45, 2 March 2022

OCA — Wed, 02 Mar 2022 07:45:36 GMT

←Older revision		Revision as of 07:45, 2 March 2022
Line 3:		Line 3:
	<StructureSection load='1fq6' size='340' side='right'caption='[[1fq6]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='1fq6' size='340' side='right'caption='[[1fq6]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fq6]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQ6 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1FQ6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fq6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FQ6 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0QF:N-[(1R)-2-{[(1R,2R,3S)-1-(CYCLOHEXYLMETHYL)-2,3-DIHYDROXY-5-METHYLHEXYL]AMINO}-1-(ETHYLSULFANYL)-2-OXOETHYL]-NALPHA-(MORPHOLIN-4-YLSULFONYL)-D-PHENYLALANINAMIDE'>0QF</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA~~</scene>, <scene name='pdbligand=GUP:ALPHA-L-GULOPYRANOSIDE'>GUP~~</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=~~NDG~~:2-~~(ACETYLAMINO)~~-~~2-DEOXY-A-D-GLUCOPYRANOSE~~'>~~NDG~~</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0QF:N-[(1R)-2-{[(1R,2R,3S)-1-(CYCLOHEXYLMETHYL)-2,3-DIHYDROXY-5-METHYLHEXYL]AMINO}-1-(ETHYLSULFANYL)-2-OXOETHYL]-NALPHA-(MORPHOLIN-4-YLSULFONYL)-D-PHENYLALANINAMIDE'>0QF</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=GUP:ALPHA-L-GULOPYRANOSIDE'>GUP</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jxr\|2jxr]], [[1dp5\|1dp5]], [[1fq4\|1fq4]], [[1fq5\|1fq5]], [[1fq7\|1fq7]], [[1fq8\|1fq8]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2jxr\|2jxr]], [[1dp5\|1dp5]], [[1fq4\|1fq4]], [[1fq5\|1fq5]], [[1fq7\|1fq7]], [[1fq8\|1fq8]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Saccharopepsin Saccharopepsin], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.25 3.4.23.25] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Saccharopepsin Saccharopepsin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.25 3.4.23.25] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=1fq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fq6 OCA], [~~http~~://pdbe.org/1fq6 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1fq6 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1fq6 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1fq6 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=1fq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fq6 OCA], [https://pdbe.org/1fq6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fq6 RCSB], [https://www.ebi.ac.uk/pdbsum/1fq6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fq6 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CARP_YEAST CARP_YEAST]] Aspartyl protease implicated in the post-translational regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY and on itself.	+	[[https://www.uniprot.org/uniprot/CARP_YEAST CARP_YEAST]] Aspartyl protease implicated in the post-translational regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY and on itself.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 33:
	==See Also==		==See Also==
	*[[Pepsin\|Pepsin]]		*[[Pepsin\|Pepsin]]
-	*[[Proteinase\|Proteinase]]
	*[[Proteinase 3D structures\|Proteinase 3D structures]]		*[[Proteinase 3D structures\|Proteinase 3D structures]]
	== References ==		== References ==

OCA at 07:08, 27 May 2020

OCA — Wed, 27 May 2020 07:08:27 GMT

←Older revision		Revision as of 07:08, 27 May 2020
Line 3:		Line 3:
	<StructureSection load='1fq6' size='340' side='right'caption='[[1fq6]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='1fq6' size='340' side='right'caption='[[1fq6]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fq6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQ6 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1FQ6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fq6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQ6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1FQ6 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0QF:N-[(1R)-2-{[(1R,2R,3S)-1-(CYCLOHEXYLMETHYL)-2,3-DIHYDROXY-5-METHYLHEXYL]AMINO}-1-(ETHYLSULFANYL)-2-OXOETHYL]-NALPHA-(MORPHOLIN-4-YLSULFONYL)-D-PHENYLALANINAMIDE'>0QF</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GUP:ALPHA-L-GULOPYRANOSIDE'>GUP</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0QF:N-[(1R)-2-{[(1R,2R,3S)-1-(CYCLOHEXYLMETHYL)-2,3-DIHYDROXY-5-METHYLHEXYL]AMINO}-1-(ETHYLSULFANYL)-2-OXOETHYL]-NALPHA-(MORPHOLIN-4-YLSULFONYL)-D-PHENYLALANINAMIDE'>0QF</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GUP:ALPHA-L-GULOPYRANOSIDE'>GUP</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jxr\|2jxr]], [[1dp5\|1dp5]], [[1fq4\|1fq4]], [[1fq5\|1fq5]], [[1fq7\|1fq7]], [[1fq8\|1fq8]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jxr\|2jxr]], [[1dp5\|1dp5]], [[1fq4\|1fq4]], [[1fq5\|1fq5]], [[1fq7\|1fq7]], [[1fq8\|1fq8]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Saccharopepsin Saccharopepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.25 3.4.23.25] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Saccharopepsin Saccharopepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.25 3.4.23.25] </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=1fq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fq6 OCA], [http://pdbe.org/1fq6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fq6 RCSB], [http://www.ebi.ac.uk/pdbsum/1fq6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fq6 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1fq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fq6 OCA], [http://pdbe.org/1fq6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fq6 RCSB], [http://www.ebi.ac.uk/pdbsum/1fq6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fq6 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 34:		Line 34:
	*[[Pepsin\|Pepsin]]		*[[Pepsin\|Pepsin]]
	*[[Proteinase\|Proteinase]]		*[[Proteinase\|Proteinase]]
		+	*[[Proteinase 3D structures\|Proteinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:00, 19 June 2019

OCA — Wed, 19 Jun 2019 07:00:39 GMT

←Older revision		Revision as of 07:00, 19 June 2019
Line 1:		Line 1:

	==X-RAY STRUCTURE OF GLYCOL INHIBITOR PD-133,450 BOUND TO SACCHAROPEPSIN==		==X-RAY STRUCTURE OF GLYCOL INHIBITOR PD-133,450 BOUND TO SACCHAROPEPSIN==
-	<StructureSection load='1fq6' size='340' side='right' caption='[[1fq6]], [[Resolution\|resolution]] 2.70Å' scene=''>	+	<StructureSection load='1fq6' size='340' side='right'caption='[[1fq6]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1fq6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FQ6 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1fq6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FQ6 FirstGlance]. <br>
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fq/1fq6_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fq/1fq6_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 33:		Line 33:
	==See Also==		==See Also==
	*[[Pepsin\|Pepsin]]		*[[Pepsin\|Pepsin]]
		+	*[[Proteinase\|Proteinase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]
	[[Category: Saccharopepsin]]		[[Category: Saccharopepsin]]

OCA at 10:51, 13 September 2017

OCA — Wed, 13 Sep 2017 10:51:52 GMT

←Older revision		Revision as of 10:51, 13 September 2017
Line 1:		Line 1:
		+
	==X-RAY STRUCTURE OF GLYCOL INHIBITOR PD-133,450 BOUND TO SACCHAROPEPSIN==		==X-RAY STRUCTURE OF GLYCOL INHIBITOR PD-133,450 BOUND TO SACCHAROPEPSIN==
	<StructureSection load='1fq6' size='340' side='right' caption='[[1fq6]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='1fq6' size='340' side='right' caption='[[1fq6]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1fq6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FQ6 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1fq6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FQ6 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0QF:N-[(1R)-2-{[(1R,2R,3S)-1-(CYCLOHEXYLMETHYL)-2,3-DIHYDROXY-5-METHYLHEXYL]AMINO}-1-(ETHYLSULFANYL)-2-OXOETHYL]-NALPHA-(MORPHOLIN-4-YLSULFONYL)-D-PHENYLALANINAMIDE'>0QF</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=~~NDG~~:2-~~(ACETYLAMINO)~~-~~2-DEOXY-A-D-GLUCOPYRANOSE~~'>~~NDG~~</scene>, <scene name='pdbligand=~~GUP~~:~~ALPHA~~-L-~~GULOPYRANOSIDE~~'>~~GUP~~</scene>, <scene name='pdbligand=~~NAG~~:N-~~ACETYL~~-D-~~GLUCOSAMINE~~'>~~NAG~~</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0QF:N-[(1R)-2-{[(1R,2R,3S)-1-(CYCLOHEXYLMETHYL)-2,3-DIHYDROXY-5-METHYLHEXYL]AMINO}-1-(ETHYLSULFANYL)-2-OXOETHYL]-NALPHA-(MORPHOLIN-4-YLSULFONYL)-D-PHENYLALANINAMIDE'>0QF</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GUP:ALPHA-L-GULOPYRANOSIDE'>GUP</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jxr\|2jxr]], [[1dp5\|1dp5]], [[1fq4\|1fq4]], [[1fq5\|1fq5]], [[1fq7\|1fq7]], [[1fq8\|1fq8]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jxr\|2jxr]], [[1dp5\|1dp5]], [[1fq4\|1fq4]], [[1fq5\|1fq5]], [[1fq7\|1fq7]], [[1fq8\|1fq8]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Saccharopepsin Saccharopepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.25 3.4.23.25] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Saccharopepsin Saccharopepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.25 3.4.23.25] </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=1fq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fq6 OCA], [http://pdbe.org/1fq6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fq6 RCSB], [http://www.ebi.ac.uk/pdbsum/1fq6 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=1fq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fq6 OCA], [http://pdbe.org/1fq6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fq6 RCSB], [http://www.ebi.ac.uk/pdbsum/1fq6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fq6 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fq6 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 09:51, 11 September 2015

OCA — Fri, 11 Sep 2015 09:51:14 GMT

←Older revision		Revision as of 09:51, 11 September 2015
Line 6:		Line 6:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jxr\|2jxr]], [[1dp5\|1dp5]], [[1fq4\|1fq4]], [[1fq5\|1fq5]], [[1fq7\|1fq7]], [[1fq8\|1fq8]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jxr\|2jxr]], [[1dp5\|1dp5]], [[1fq4\|1fq4]], [[1fq5\|1fq5]], [[1fq7\|1fq7]], [[1fq8\|1fq8]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Saccharopepsin Saccharopepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.25 3.4.23.25] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Saccharopepsin Saccharopepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.25 3.4.23.25] </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=1fq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fq6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fq6 RCSB], [http://www.ebi.ac.uk/pdbsum/1fq6 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=1fq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fq6 OCA], [http://pdbe.org/1fq6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fq6 RCSB], [http://www.ebi.ac.uk/pdbsum/1fq6 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 28:
	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 1fq6" style="background-color:#fffaf0;"></div>

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

OCA at 14:45, 25 December 2014

OCA — Thu, 25 Dec 2014 14:45:27 GMT

←Older revision		Revision as of 14:45, 25 December 2014
Line 8:		Line 8:
	<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=1fq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fq6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fq6 RCSB], [http://www.ebi.ac.uk/pdbsum/1fq6 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=1fq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fq6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fq6 RCSB], [http://www.ebi.ac.uk/pdbsum/1fq6 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CARP_YEAST CARP_YEAST]] Aspartyl protease implicated in the post-translational regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY and on itself.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 00:17, 23 December 2014

OCA — Tue, 23 Dec 2014 00:17:42 GMT

←Older revision		Revision as of 00:17, 23 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1fq6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FQ6 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1fq6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FQ6 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0QF:N-[(1R)-2-{[(1R,2R,3S)-1-(CYCLOHEXYLMETHYL)-2,3-DIHYDROXY-5-METHYLHEXYL]AMINO}-1-(ETHYLSULFANYL)-2-OXOETHYL]-NALPHA-(MORPHOLIN-4-YLSULFONYL)-D-PHENYLALANINAMIDE'>0QF</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=GUP:ALPHA-L-GULOPYRANOSIDE'>GUP</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0QF:N-[(1R)-2-{[(1R,2R,3S)-1-(CYCLOHEXYLMETHYL)-2,3-DIHYDROXY-5-METHYLHEXYL]AMINO}-1-(ETHYLSULFANYL)-2-OXOETHYL]-NALPHA-(MORPHOLIN-4-YLSULFONYL)-D-PHENYLALANINAMIDE'>0QF</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=GUP:ALPHA-L-GULOPYRANOSIDE'>GUP</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jxr\|2jxr]], [[1dp5\|1dp5]], [[1fq4\|1fq4]], [[1fq5\|1fq5]], [[1fq7\|1fq7]], [[1fq8\|1fq8]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jxr\|2jxr]], [[1dp5\|1dp5]], [[1fq4\|1fq4]], [[1fq5\|1fq5]], [[1fq7\|1fq7]], [[1fq8\|1fq8]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Saccharopepsin Saccharopepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.25 3.4.23.25] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Saccharopepsin Saccharopepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.25 3.4.23.25] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fq6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fq6 RCSB], [http://www.ebi.ac.uk/pdbsum/1fq6 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=1fq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fq6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fq6 RCSB], [http://www.ebi.ac.uk/pdbsum/1fq6 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 35:
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]
	[[Category: Saccharopepsin]]		[[Category: Saccharopepsin]]
-	[[Category: Badasso, M O.]]	+	[[Category: Badasso, M O]]
-	[[Category: Cooper, J B.]]	+	[[Category: Cooper, J B]]
-	[[Category: Cronin, N B.]]	+	[[Category: Cronin, N B]]
-	[[Category: Dreyer, T.]]	+	[[Category: Dreyer, T]]
-	[[Category: Hoover, D J.]]	+	[[Category: Hoover, D J]]
-	[[Category: Humblet, C C.]]	+	[[Category: Humblet, C C]]
-	[[Category: Lunney, E A.]]	+	[[Category: Lunney, E A]]
-	[[Category: Rosati, R L.]]	+	[[Category: Rosati, R L]]
-	[[Category: Tickle, I J.]]	+	[[Category: Tickle, I J]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Hydrolase-hydrolase inhibitor complex]]		[[Category: Hydrolase-hydrolase inhibitor complex]]

OCA at 17:22, 29 September 2014

OCA — Mon, 29 Sep 2014 17:22:28 GMT

←Older revision		Revision as of 17:22, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1fq6.~~png~~\|~~left~~\|200px]]	+	==X-RAY STRUCTURE OF GLYCOL INHIBITOR PD-133,450 BOUND TO SACCHAROPEPSIN==
		+	<StructureSection load='1fq6' size='340' side='right' caption='[[1fq6]], [[Resolution\|resolution]] 2.70Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1fq6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FQ6 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0QF:N-[(1R)-2-{[(1R,2R,3S)-1-(CYCLOHEXYLMETHYL)-2,3-DIHYDROXY-5-METHYLHEXYL]AMINO}-1-(ETHYLSULFANYL)-2-OXOETHYL]-NALPHA-(MORPHOLIN-4-YLSULFONYL)-D-PHENYLALANINAMIDE'>0QF</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=GUP:ALPHA-L-GULOPYRANOSIDE'>GUP</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jxr\|2jxr]], [[1dp5\|1dp5]], [[1fq4\|1fq4]], [[1fq5\|1fq5]], [[1fq7\|1fq7]], [[1fq8\|1fq8]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Saccharopepsin Saccharopepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.25 3.4.23.25] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fq6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fq6 RCSB], [http://www.ebi.ac.uk/pdbsum/1fq6 PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fq/1fq6_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Saccharopepsin is a vacuolar aspartic proteinase involved in activation of a number of hydrolases. The enzyme has great structural homology to mammalian aspartic proteinases including human renin and we have used it as a model system to study the binding of renin inhibitors by X-ray crystallography. Five medium-to-high resolution structures of saccharopepsin complexed with transition-state analogue renin inhibitors were determined. The structure of a cyclic peptide inhibitor (PD-129,541) complexed with the proteinase was solved to 2.5 A resolution. This inhibitor has low affinity for human renin yet binds very tightly to the yeast proteinase (K(i)=4 nM). The high affinity of this inhibitor can be attributed to its bulky cyclic moiety spanning P(2)-P(3)' and other residues that appear to optimally fit the binding sub-sites of the enzyme. Superposition of the saccharopepsin structure on that of renin showed that a movement of the loop 286-301 relative to renin facilitates tighter binding of this inhibitor to saccharopepsin. Our 2.8 A resolution structure of the complex with CP-108,420 shows that its benzimidazole P(3 )replacement retains one of the standard hydrogen bonds that normally involve the inhibitor's main-chain. This suggests a non-peptide lead in overcoming the problem of susceptible peptide bonds in the design of aspartic proteinase inhibitors. CP-72,647 which possesses a basic histidine residue at P(2), has a high affinity for renin (K(i)=5 nM) but proves to be a poor inhibitor for saccharopepsin (K(i)=3.7 microM). This may stem from the fact that the histidine residue would not bind favourably with the predominantly hydrophobic S(2) sub-site of saccharopepsin.

-	~~{{STRUCTURE_1fq6\| PDB=1fq6 \| SCENE= }}~~	+	X-ray structures of five renin inhibitors bound to saccharopepsin: exploration of active-site specificity.,Cronin NB, Badasso MO, J Tickle I, Dreyer T, Hoover DJ, Rosati RL, Humblet CC, Lunney EA, Cooper JB J Mol Biol. 2000 Nov 10;303(5):745-60. PMID:11061973<ref>PMID:11061973</ref>

-	~~===X-RAY STRUCTURE OF GLYCOL INHIBITOR PD-133~~,~~450 BOUND TO SACCHAROPEPSIN===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_11061973}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1fq6]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1FQ6 OCA].~~	+

	==See Also==		==See Also==
	*[[Pepsin\|Pepsin]]		*[[Pepsin\|Pepsin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:011061973<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]
	[[Category: Saccharopepsin]]		[[Category: Saccharopepsin]]

OCA at 17:58, 20 October 2012

OCA — Sat, 20 Oct 2012 17:58:13 GMT

←Older revision		Revision as of 17:58, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1fq6]] is a 1 chain structure ~~of [[Pepsin]]~~ with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQ6 OCA].	+	[[1fq6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQ6 OCA].

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