1id4 - Revision history

OCA at 07:34, 7 February 2024

2024-02-07T07:34:11Z

←Older revision		Revision as of 07:34, 7 February 2024
Line 3:		Line 3:
	<StructureSection load='1id4' size='340' side='right'caption='[[1id4]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='1id4' size='340' side='right'caption='[[1id4]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1id4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Hcmva Hcmva~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ID4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ID4 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1id4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_herpesvirus_5_strain_AD169 Human herpesvirus 5 strain AD169]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ID4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ID4 FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[1ieg\|1ieg]], [[1ief\|1ief]], [[1ied\|1ied]], [[1iec\|1iec]], [[1wpo\|1wpo]], [[2wpo\|2wpo]]</div></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]] 2.2Å</td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Gene~~\|~~Gene:~~]]~~</b></td><td class="sblockDat">UL80 ([https://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=10360 HCMVA])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Assemblin Assemblin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.97 3.4.21.97] </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=1id4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1id4 OCA], [https://pdbe.org/1id4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1id4 RCSB], [https://www.ebi.ac.uk/pdbsum/1id4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1id4 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=1id4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1id4 OCA], [https://pdbe.org/1id4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1id4 RCSB], [https://www.ebi.ac.uk/pdbsum/1id4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1id4 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/SCAF_HCMVA SCAF_HCMVA]] Capsid scaffolding protein acts as a scaffold protein by binding major capsid protein UL86 in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein UL86. Cleavages products are evicted from the capsid before or during DNA packaging (By similarity). Assemblin is a protease essential for virion assembly in the nucleus. Catalyzes the cleavage of the assembly protein after complete capsid formation. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging (By similarity). Assembly protein plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein UL86. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging (By similarity).	+	[https://www.uniprot.org/uniprot/SCAF_HCMVA SCAF_HCMVA] Capsid scaffolding protein acts as a scaffold protein by binding major capsid protein UL86 in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein UL86. Cleavages products are evicted from the capsid before or during DNA packaging (By similarity). Assemblin is a protease essential for virion assembly in the nucleus. Catalyzes the cleavage of the assembly protein after complete capsid formation. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging (By similarity). Assembly protein plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein UL86. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 21:		Line 19:
	</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=1id4 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=1id4 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Herpesvirus proteases belong to a new class of serine proteases and contain a novel Ser-His-His catalytic triad, while classical serine proteases have an acidic residue as the third member. To gain a better understanding of the molecular basis for the functional role of the third-member His residue, we have carried out structural and biochemical investigations of human cytomegalovirus (HCMV) protease that bears mutations of the His157 third member. Kinetic studies showed that all the mutants have reduced catalytic activity. Structural studies revealed that a solvent molecule is hydrogen-bonded to the His63 second member and Ser134 in the H157A mutant, partly rescuing the activity of this mutant. This is confirmed by our kinetic and structural observations on the S134A/H157A double mutant, which showed further reductions in the catalytic activity. The structure of the H157A mutant is also in complex with the PMSF inhibitor. The H157E mutant has the best catalytic activity among the mutants; its structure, however, showed conformational readjustments of the His63 and Ser132 residues. The Ser132-His63 diad of HCMV protease has similar activity as the diads in classical serine proteases, whereas the contribution of the His157 third member to the catalysis is much smaller. Finally, structural comparisons revealed the presence of two conserved structural water molecules at the bottom of the S(1) pocket, suggesting a possible new direction for the design of HCMV protease inhibitors.
-
-	Investigating the role of histidine 157 in the catalytic activity of human cytomegalovirus protease.,Khayat R, Batra R, Massariol MJ, Lagace L, Tong L Biochemistry. 2001 May 29;40(21):6344-51. PMID:11371196<ref>PMID:11371196</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1id4" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Virus protease 3D structures\|Virus protease 3D structures]]		*[[Virus protease 3D structures\|Virus protease 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Assemblin]]~~	+	[[Category: Human herpesvirus 5 strain AD169]]
-	~~[[Category: Hcmva~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Batra, R]]	+	[[Category: Batra R]]
-	[[Category: Khayat, R]]	+	[[Category: Khayat R]]
-	[[Category: Lagace, L]]	+	[[Category: Lagace L]]
-	[[Category: Massariol~~, M J~~]]	+	[[Category: Massariol MJ]]
-	[[Category: Tong, L]]	+	[[Category: Tong L]]
-	~~[[Category: Coat protein]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Phosphorylation]]~~	+
-	~~[[Category: Serine protease]]~~	+
-	~~[[Category: Viral protease~~]]	+

OCA at 14:25, 27 October 2021

2021-10-27T14:25:59Z

←Older revision		Revision as of 14:25, 27 October 2021
Line 3:		Line 3:
	<StructureSection load='1id4' size='340' side='right'caption='[[1id4]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='1id4' size='340' side='right'caption='[[1id4]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1id4]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Hcmva Hcmva]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ID4 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1ID4 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1id4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Hcmva Hcmva]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ID4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ID4 FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ieg\|1ieg]], [[1ief\|1ief]], [[1ied\|1ied]], [[1iec\|1iec]], [[1wpo\|1wpo]], [[2wpo\|2wpo]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ieg\|1ieg]], [[1ief\|1ief]], [[1ied\|1ied]], [[1iec\|1iec]], [[1wpo\|1wpo]], [[2wpo\|2wpo]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UL80 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10360 HCMVA])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UL80 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10360 HCMVA])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Assemblin Assemblin], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.97 3.4.21.97] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Assemblin Assemblin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.97 3.4.21.97] </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=1id4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1id4 OCA], [~~http~~://pdbe.org/1id4 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1id4 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1id4 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1id4 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=1id4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1id4 OCA], [https://pdbe.org/1id4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1id4 RCSB], [https://www.ebi.ac.uk/pdbsum/1id4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1id4 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/SCAF_HCMVA SCAF_HCMVA]] Capsid scaffolding protein acts as a scaffold protein by binding major capsid protein UL86 in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein UL86. Cleavages products are evicted from the capsid before or during DNA packaging (By similarity). Assemblin is a protease essential for virion assembly in the nucleus. Catalyzes the cleavage of the assembly protein after complete capsid formation. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging (By similarity). Assembly protein plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein UL86. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging (By similarity).	+	[[https://www.uniprot.org/uniprot/SCAF_HCMVA SCAF_HCMVA]] Capsid scaffolding protein acts as a scaffold protein by binding major capsid protein UL86 in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein UL86. Cleavages products are evicted from the capsid before or during DNA packaging (By similarity). Assemblin is a protease essential for virion assembly in the nucleus. Catalyzes the cleavage of the assembly protein after complete capsid formation. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging (By similarity). Assembly protein plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein UL86. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 10:37, 18 November 2020

2020-11-18T10:37:59Z

←Older revision		Revision as of 10:37, 18 November 2020
Line 1:		Line 1:

	==CRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT (H157Q) OF THE HUMAN CYTOMEGALOVIRUS PROTEASE==		==CRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT (H157Q) OF THE HUMAN CYTOMEGALOVIRUS PROTEASE==
-	<StructureSection load='1id4' size='340' side='right' caption='[[1id4]], [[Resolution\|resolution]] 2.20Å' scene=''>	+	<StructureSection load='1id4' size='340' side='right'caption='[[1id4]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1id4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Hcmva Hcmva]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ID4 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1ID4 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1id4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Hcmva Hcmva]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ID4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1ID4 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ieg\|1ieg]], [[1ief\|1ief]], [[1ied\|1ied]], [[1iec\|1iec]], [[1wpo\|1wpo]], [[2wpo\|2wpo]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ieg\|1ieg]], [[1ief\|1ief]], [[1ied\|1ied]], [[1iec\|1iec]], [[1wpo\|1wpo]], [[2wpo\|2wpo]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UL80 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10360 HCMVA])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UL80 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10360 HCMVA])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Assemblin Assemblin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.97 3.4.21.97] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Assemblin Assemblin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.97 3.4.21.97] </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=1id4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1id4 OCA], [http://pdbe.org/1id4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1id4 RCSB], [http://www.ebi.ac.uk/pdbsum/1id4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1id4 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=1id4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1id4 OCA], [http://pdbe.org/1id4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1id4 RCSB], [http://www.ebi.ac.uk/pdbsum/1id4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1id4 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1id4" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1id4" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Virus protease 3D structures\|Virus protease 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 36:		Line 39:
	[[Category: Assemblin]]		[[Category: Assemblin]]
	[[Category: Hcmva]]		[[Category: Hcmva]]
		+	[[Category: Large Structures]]
	[[Category: Batra, R]]		[[Category: Batra, R]]
	[[Category: Khayat, R]]		[[Category: Khayat, R]]

OCA at 09:36, 10 January 2018

2018-01-10T09:36:37Z

←Older revision		Revision as of 09:36, 10 January 2018
Line 1:		Line 1:
		+
	==CRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT (H157Q) OF THE HUMAN CYTOMEGALOVIRUS PROTEASE==		==CRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT (H157Q) OF THE HUMAN CYTOMEGALOVIRUS PROTEASE==
	<StructureSection load='1id4' size='340' side='right' caption='[[1id4]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='1id4' size='340' side='right' caption='[[1id4]], [[Resolution\|resolution]] 2.20Å' scene=''>
Line 6:		Line 7:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UL80 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10360 HCMVA])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UL80 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10360 HCMVA])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Assemblin Assemblin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.97 3.4.21.97] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Assemblin Assemblin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.97 3.4.21.97] </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=1id4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1id4 OCA], [http://pdbe.org/1id4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1id4 RCSB], [http://www.ebi.ac.uk/pdbsum/1id4 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=1id4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1id4 OCA], [http://pdbe.org/1id4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1id4 RCSB], [http://www.ebi.ac.uk/pdbsum/1id4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1id4 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/id/1id4_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/id/1id4_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>

OCA at 05:21, 9 February 2016

2016-02-09T05:21:59Z

←Older revision		Revision as of 05:21, 9 February 2016
Line 18:		Line 18:
	<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=1id4 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 19:02, 10 September 2015

2015-09-10T19:02:05Z

←Older revision		Revision as of 19:02, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1id4' size='340' side='right' caption='[[1id4]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='1id4' size='340' side='right' caption='[[1id4]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1id4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Human_herpesvirus_5 Human herpesvirus 5~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ID4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ID4 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1id4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Hcmva Hcmva]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ID4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ID4 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ieg\|1ieg]], [[1ief\|1ief]], [[1ied\|1ied]], [[1iec\|1iec]], [[1wpo\|1wpo]], [[2wpo\|2wpo]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ieg\|1ieg]], [[1ief\|1ief]], [[1ied\|1ied]], [[1iec\|1iec]], [[1wpo\|1wpo]], [[2wpo\|2wpo]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UL80 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=~~10359 Human herpesvirus 5~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UL80 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10360 HCMVA])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Assemblin Assemblin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.97 3.4.21.97] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Assemblin Assemblin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.97 3.4.21.97] </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=1id4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1id4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1id4 RCSB], [http://www.ebi.ac.uk/pdbsum/1id4 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=1id4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1id4 OCA], [http://pdbe.org/1id4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1id4 RCSB], [http://www.ebi.ac.uk/pdbsum/1id4 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/~~VP40_HCMVA VP40_HCMVA~~]] Capsid scaffolding protein acts as a scaffold protein by binding major capsid protein UL86 in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein UL86. Cleavages products are evicted from the capsid before or during DNA packaging (By similarity). Assemblin is a protease essential for virion assembly in the nucleus. Catalyzes the cleavage of the assembly protein after complete capsid formation. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging (By similarity). Assembly protein plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein UL86. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging (By similarity).	+	[[http://www.uniprot.org/uniprot/SCAF_HCMVA SCAF_HCMVA]] Capsid scaffolding protein acts as a scaffold protein by binding major capsid protein UL86 in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein UL86. Cleavages products are evicted from the capsid before or during DNA packaging (By similarity). Assemblin is a protease essential for virion assembly in the nucleus. Catalyzes the cleavage of the assembly protein after complete capsid formation. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging (By similarity). Assembly protein plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein UL86. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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 1id4" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 33:		Line 34:
	</StructureSection>		</StructureSection>
	[[Category: Assemblin]]		[[Category: Assemblin]]
-	[[Category: ~~Human herpesvirus 5~~]]	+	[[Category: Hcmva]]
	[[Category: Batra, R]]		[[Category: Batra, R]]
	[[Category: Khayat, R]]		[[Category: Khayat, R]]

OCA at 04:43, 25 December 2014

2014-12-25T04:43:21Z

←Older revision		Revision as of 04:43, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1id4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_5 Human herpesvirus 5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ID4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ID4 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1id4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_5 Human herpesvirus 5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ID4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ID4 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ieg\|1ieg]], [[1ief\|1ief]], [[1ied\|1ied]], [[1iec\|1iec]], [[1wpo\|1wpo]], [[2wpo\|2wpo]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ieg\|1ieg]], [[1ief\|1ief]], [[1ied\|1ied]], [[1iec\|1iec]], [[1wpo\|1wpo]], [[2wpo\|2wpo]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UL80 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10359 Human herpesvirus 5])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UL80 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10359 Human herpesvirus 5])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Assemblin Assemblin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.97 3.4.21.97] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Assemblin Assemblin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.97 3.4.21.97] </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=1id4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1id4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1id4 RCSB], [http://www.ebi.ac.uk/pdbsum/1id4 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=1id4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1id4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1id4 RCSB], [http://www.ebi.ac.uk/pdbsum/1id4 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/VP40_HCMVA VP40_HCMVA]] Capsid scaffolding protein acts as a scaffold protein by binding major capsid protein UL86 in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein UL86. Cleavages products are evicted from the capsid before or during DNA packaging (By similarity). Assemblin is a protease essential for virion assembly in the nucleus. Catalyzes the cleavage of the assembly protein after complete capsid formation. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging (By similarity). Assembly protein plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein UL86. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 34:
	[[Category: Assemblin]]		[[Category: Assemblin]]
	[[Category: Human herpesvirus 5]]		[[Category: Human herpesvirus 5]]
-	[[Category: Batra, R.]]	+	[[Category: Batra, R]]
-	[[Category: Khayat, R.]]	+	[[Category: Khayat, R]]
-	[[Category: Lagace, L.]]	+	[[Category: Lagace, L]]
-	[[Category: Massariol, M J.]]	+	[[Category: Massariol, M J]]
-	[[Category: Tong, L.]]	+	[[Category: Tong, L]]
	[[Category: Coat protein]]		[[Category: Coat protein]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 11:34, 28 September 2014

2014-09-28T11:34:12Z

←Older revision		Revision as of 11:34, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1id4.~~png~~\|~~left~~\|200px]]	+	==CRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT (H157Q) OF THE HUMAN CYTOMEGALOVIRUS PROTEASE==
		+	<StructureSection load='1id4' size='340' side='right' caption='[[1id4]], [[Resolution\|resolution]] 2.20Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1id4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_5 Human herpesvirus 5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ID4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ID4 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ieg\|1ieg]], [[1ief\|1ief]], [[1ied\|1ied]], [[1iec\|1iec]], [[1wpo\|1wpo]], [[2wpo\|2wpo]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UL80 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10359 Human herpesvirus 5])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Assemblin Assemblin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.97 3.4.21.97] </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=1id4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1id4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1id4 RCSB], [http://www.ebi.ac.uk/pdbsum/1id4 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/id/1id4_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 ==
		+	Herpesvirus proteases belong to a new class of serine proteases and contain a novel Ser-His-His catalytic triad, while classical serine proteases have an acidic residue as the third member. To gain a better understanding of the molecular basis for the functional role of the third-member His residue, we have carried out structural and biochemical investigations of human cytomegalovirus (HCMV) protease that bears mutations of the His157 third member. Kinetic studies showed that all the mutants have reduced catalytic activity. Structural studies revealed that a solvent molecule is hydrogen-bonded to the His63 second member and Ser134 in the H157A mutant, partly rescuing the activity of this mutant. This is confirmed by our kinetic and structural observations on the S134A/H157A double mutant, which showed further reductions in the catalytic activity. The structure of the H157A mutant is also in complex with the PMSF inhibitor. The H157E mutant has the best catalytic activity among the mutants; its structure, however, showed conformational readjustments of the His63 and Ser132 residues. The Ser132-His63 diad of HCMV protease has similar activity as the diads in classical serine proteases, whereas the contribution of the His157 third member to the catalysis is much smaller. Finally, structural comparisons revealed the presence of two conserved structural water molecules at the bottom of the S(1) pocket, suggesting a possible new direction for the design of HCMV protease inhibitors.

-	~~{{STRUCTURE_1id4\| PDB=1id4 \| SCENE= }}~~	+	Investigating the role of histidine 157 in the catalytic activity of human cytomegalovirus protease.,Khayat R, Batra R, Massariol MJ, Lagace L, Tong L Biochemistry. 2001 May 29;40(21):6344-51. PMID:11371196<ref>PMID:11371196</ref>

-	~~===CRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT (H157Q) OF THE HUMAN CYTOMEGALOVIRUS PROTEASE===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_11371196}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1id4]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Human_herpesvirus_5 Human herpesvirus 5]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1ID4 OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:011371196<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Assemblin]]		[[Category: Assemblin]]
	[[Category: Human herpesvirus 5]]		[[Category: Human herpesvirus 5]]

OCA: Protected "1id4" [edit=sysop:move=sysop]

2012-11-28T15:17:16Z

Protected "1id4" [edit=sysop:move=sysop]

←Older revision

Revision as of 15:17, 28 November 2012

OCA at 15:17, 28 November 2012

2012-11-28T15:17:13Z

←Older revision		Revision as of 15:17, 28 November 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1id4.png\|left\|200px]]		[[Image:1id4.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1id4", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_1id4\| PDB=1id4 \| SCENE= }}		{{STRUCTURE_1id4\| PDB=1id4 \| SCENE= }}

	===CRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT (H157Q) OF THE HUMAN CYTOMEGALOVIRUS PROTEASE===		===CRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT (H157Q) OF THE HUMAN CYTOMEGALOVIRUS PROTEASE===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_11371196}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 11371196 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_11371196}}		{{ABSTRACT_PUBMED_11371196}}

	==About this Structure==		==About this Structure==
-	~~1ID4~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Human_herpesvirus_5 Human herpesvirus 5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ID4 OCA].	+	[[1id4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_5 Human herpesvirus 5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ID4 OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~11371196~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:011371196</ref><references group="xtra"/>
	[[Category: Assemblin]]		[[Category: Assemblin]]
	[[Category: Human herpesvirus 5]]		[[Category: Human herpesvirus 5]]
Line 36:		Line 24:
	[[Category: Serine protease]]		[[Category: Serine protease]]
	[[Category: Viral protease]]		[[Category: Viral protease]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 06:47:59 2009''