4pqa - Revision history

OCA at 12:42, 1 March 2024

OCA — Fri, 01 Mar 2024 12:42:30 GMT

←Older revision		Revision as of 12:42, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4pqa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_MC58 Neisseria meningitidis MC58]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PQA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PQA FirstGlance]. <br>		<table><tr><td colspan='2'>[[4pqa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_MC58 Neisseria meningitidis MC58]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PQA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PQA FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=X8Z:L-CAPTOPRIL'>X8Z</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.78Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=X8Z:L-CAPTOPRIL'>X8Z</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4pqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pqa OCA], [https://pdbe.org/4pqa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pqa RCSB], [https://www.ebi.ac.uk/pdbsum/4pqa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pqa 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=4pqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pqa OCA], [https://pdbe.org/4pqa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pqa RCSB], [https://www.ebi.ac.uk/pdbsum/4pqa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pqa ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/DAPE_NEIMB DAPE_NEIMB] Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls (By similarity).[HAMAP-Rule:MF_01690]		[https://www.uniprot.org/uniprot/DAPE_NEIMB DAPE_NEIMB] Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls (By similarity).[HAMAP-Rule:MF_01690]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Binding of the competitive inhibitor L-captopril to the dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase from Neisseria meningitidis (NmDapE) was examined by kinetic, spectroscopic, and crystallographic methods. L-Captopril, an angiotensin-converting enzyme (ACE) inhibitor, was previously shown to be a potent inhibitor of the DapE from Haemophilus influenzae (HiDapE) with an IC50 of 3.3 muM and a measured Ki of 1.8 muM and displayed a dose-responsive antibiotic activity toward Escherichia coli. L-Captopril is also a competitive inhibitor of NmDapE with a Ki of 2.8 muM. To examine the nature of the interaction of L-captopril with the dinuclear active site of DapE, we have obtained electron paramagnetic resonance (EPR) and magnetic circular dichroism (MCD) data for the enzymatically hyperactive Co(II)-substituted forms of both HiDapE and NmDapE. EPR and MCD data indicate that the two Co(II) ions in DapE are antiferromagnetically coupled, yielding an S = 0 ground state, and suggest a thiolate bridge between the two metal ions. Verification of a thiolate-bridged dinuclear complex was obtained by determining the three-dimensional X-ray crystal structure of NmDapE in complex with L-captopril at 1.8 A resolution. Combination of these data provides new insights into binding of L-captopril to the active site of DapE enzymes as well as important inhibitor-active site residue interaction's. Such information is critical for the design of new, potent inhibitors of DapE enzymes.
-
-	Inhibition of the dapE-Encoded N-Succinyl-L,L-diaminopimelic Acid Desuccinylase from Neisseria meningitidis by L-Captopril.,Starus A, Nocek B, Bennett B, Larrabee JA, Shaw DL, Sae-Lee W, Russo MT, Gillner DM, Makowska-Grzyska M, Joachimiak A, Holz RC Biochemistry. 2015 Aug 11;54(31):4834-44. doi: 10.1021/acs.biochem.5b00475. Epub , 2015 Aug 3. PMID:26186504<ref>PMID:26186504</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4pqa" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 07:24, 8 February 2023

OCA — Wed, 08 Feb 2023 07:24:22 GMT

←Older revision		Revision as of 07:24, 8 February 2023
Line 1:		Line 1:
		+
	==Crystal Structure of succinyl-diaminopimelate desuccinylase from Neisseria meningitidis MC58 in complex with the Inhibitor Captopril==		==Crystal Structure of succinyl-diaminopimelate desuccinylase from Neisseria meningitidis MC58 in complex with the Inhibitor Captopril==
-	<StructureSection load='4pqa' size='340' side='right' caption='[[4pqa]], [[Resolution\|resolution]] 1.78Å' scene=''>	+	<StructureSection load='4pqa' size='340' side='right'caption='[[4pqa]], [[Resolution\|resolution]] 1.78Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4pqa]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Neimb Neimb~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PQA OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4PQA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4pqa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_MC58 Neisseria meningitidis MC58]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PQA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PQA FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=X8Z:L-CAPTOPRIL'>X8Z</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=X8Z:L-CAPTOPRIL'>X8Z</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dapE, NMB1530 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=122586 NEIMB])</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=4pqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pqa OCA], [https://pdbe.org/4pqa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pqa RCSB], [https://www.ebi.ac.uk/pdbsum/4pqa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pqa ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinyl-diaminopimelate_desuccinylase Succinyl-diaminopimelate desuccinylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.18 3.5.1.18] </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=4pqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pqa OCA], [~~http~~://pdbe.org/4pqa PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4pqa RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4pqa PDBsum]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/DAPE_NEIMB DAPE_NEIMB]] Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls (By similarity).[HAMAP-Rule:MF_01690]	+	[https://www.uniprot.org/uniprot/DAPE_NEIMB DAPE_NEIMB] Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls (By similarity).[HAMAP-Rule:MF_01690]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Neimb~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Succinyl-diaminopimelate desuccinylase~~]]	+	[[Category: Neisseria meningitidis MC58]]
-	[[Category: Anderson~~, W F]]~~	+	[[Category: Anderson WF]]
-	~~[[Category: Structural genomic~~]]	+	[[Category: Holz R]]
-	[[Category: Holz, R]]	+	[[Category: Joachimiak A]]
-	[[Category: Joachimiak, A]]	+	[[Category: Nocek B]]
-	[[Category: Nocek, B]]	+	[[Category: Starus A]]
-	[[Category: Starus, A]]	+
-	~~[[Category: Captopril]]~~	+
-	~~[[Category: Csgid]]~~	+
-	~~[[Category: Dape]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Hydrolase-hydrolase inhibitor complex]]~~	+
-	~~[[Category: M20 aminopeptidase]]~~	+
-	~~[[Category: Metaloenzyme]]~~	+
-	~~[[Category: National institute of allergy and infectious disease]]~~	+
-	~~[[Category: Niaid~~]]	+

OCA at 18:41, 27 January 2016

OCA — Wed, 27 Jan 2016 18:41:17 GMT

←Older revision		Revision as of 18:41, 27 January 2016
Line 6:		Line 6:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dapE, NMB1530 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=122586 NEIMB])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dapE, NMB1530 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=122586 NEIMB])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinyl-diaminopimelate_desuccinylase Succinyl-diaminopimelate desuccinylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.18 3.5.1.18] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinyl-diaminopimelate_desuccinylase Succinyl-diaminopimelate desuccinylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.18 3.5.1.18] </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=4pqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pqa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pqa RCSB], [http://www.ebi.ac.uk/pdbsum/4pqa 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=4pqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pqa OCA], [http://pdbe.org/4pqa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pqa RCSB], [http://www.ebi.ac.uk/pdbsum/4pqa PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/DAPE_NEIMB DAPE_NEIMB]] Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls (By similarity).[HAMAP-Rule:MF_01690]		[[http://www.uniprot.org/uniprot/DAPE_NEIMB DAPE_NEIMB]] Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls (By similarity).[HAMAP-Rule:MF_01690]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Binding of the competitive inhibitor L-captopril to the dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase from Neisseria meningitidis (NmDapE) was examined by kinetic, spectroscopic, and crystallographic methods. L-Captopril, an angiotensin-converting enzyme (ACE) inhibitor, was previously shown to be a potent inhibitor of the DapE from Haemophilus influenzae (HiDapE) with an IC50 of 3.3 muM and a measured Ki of 1.8 muM and displayed a dose-responsive antibiotic activity toward Escherichia coli. L-Captopril is also a competitive inhibitor of NmDapE with a Ki of 2.8 muM. To examine the nature of the interaction of L-captopril with the dinuclear active site of DapE, we have obtained electron paramagnetic resonance (EPR) and magnetic circular dichroism (MCD) data for the enzymatically hyperactive Co(II)-substituted forms of both HiDapE and NmDapE. EPR and MCD data indicate that the two Co(II) ions in DapE are antiferromagnetically coupled, yielding an S = 0 ground state, and suggest a thiolate bridge between the two metal ions. Verification of a thiolate-bridged dinuclear complex was obtained by determining the three-dimensional X-ray crystal structure of NmDapE in complex with L-captopril at 1.8 A resolution. Combination of these data provides new insights into binding of L-captopril to the active site of DapE enzymes as well as important inhibitor-active site residue interaction's. Such information is critical for the design of new, potent inhibitors of DapE enzymes.
		+
		+	Inhibition of the dapE-Encoded N-Succinyl-L,L-diaminopimelic Acid Desuccinylase from Neisseria meningitidis by L-Captopril.,Starus A, Nocek B, Bennett B, Larrabee JA, Shaw DL, Sae-Lee W, Russo MT, Gillner DM, Makowska-Grzyska M, Joachimiak A, Holz RC Biochemistry. 2015 Aug 11;54(31):4834-44. doi: 10.1021/acs.biochem.5b00475. Epub , 2015 Aug 3. PMID:26186504<ref>PMID:26186504</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4pqa" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
Line 19:		Line 30:
	[[Category: Joachimiak, A]]		[[Category: Joachimiak, A]]
	[[Category: Nocek, B]]		[[Category: Nocek, B]]
-	[[Category: Starus ,A]]	+	[[Category: Starus, A]]
	[[Category: Captopril]]		[[Category: Captopril]]
	[[Category: Csgid]]		[[Category: Csgid]]

OCA at 22:56, 24 December 2014

OCA — Wed, 24 Dec 2014 22:56:19 GMT

←Older revision		Revision as of 22:56, 24 December 2014
Line 2:		Line 2:
	<StructureSection load='4pqa' size='340' side='right' caption='[[4pqa]], [[Resolution\|resolution]] 1.78Å' scene=''>		<StructureSection load='4pqa' size='340' side='right' caption='[[4pqa]], [[Resolution\|resolution]] 1.78Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4pqa]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PQA OCA]. <br>	+	<table><tr><td colspan='2'>[[4pqa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Neimb Neimb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PQA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PQA FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=X8Z:L-CAPTOPRIL'>X8Z</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=X8Z:L-CAPTOPRIL'>X8Z</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/~~Glucokinase Glucokinase~~], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.~~2 2~~.7.1.2] </span></td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dapE, NMB1530 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=122586 NEIMB])</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=4pqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pqa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pqa RCSB], [http://www.ebi.ac.uk/pdbsum/4pqa PDBsum]</span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinyl-diaminopimelate_desuccinylase Succinyl-diaminopimelate desuccinylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.18 3.5.1.18] </span></td></tr>
-	<table>	+	<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=4pqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pqa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pqa RCSB], [http://www.ebi.ac.uk/pdbsum/4pqa PDBsum]</span></td></tr>
-	== ~~References~~ ==	+	</table>
-	~~<references~~/>	+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DAPE_NEIMB DAPE_NEIMB]] Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls (By similarity).[HAMAP-Rule:MF_01690]
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Neimb]]
	[[Category: Succinyl-diaminopimelate desuccinylase]]		[[Category: Succinyl-diaminopimelate desuccinylase]]
-	[[Category: Anderson, W F.]]	+	[[Category: Anderson, W F]]
-	[[Category: ~~CSGID, Center for~~ Structural ~~Genomics of Infectious Diseases.~~]]	+	[[Category: Structural genomic]]
-	[[Category: Holz, R.]]	+	[[Category: Holz, R]]
-	[[Category: Joachimiak, A.]]	+	[[Category: Joachimiak, A]]
-	[[Category: Nocek, B.]]	+	[[Category: Nocek, B]]
-	[[Category: Starus ,A.]]	+	[[Category: Starus ,A]]
	[[Category: Captopril]]		[[Category: Captopril]]
-	[[Category: Center for structural genomics of infectious disease]]
	[[Category: Csgid]]		[[Category: Csgid]]
	[[Category: Dape]]		[[Category: Dape]]
Line 28:		Line 29:
	[[Category: National institute of allergy and infectious disease]]		[[Category: National institute of allergy and infectious disease]]
	[[Category: Niaid]]		[[Category: Niaid]]
-	[[Category: Structural genomic]]

OCA at 09:31, 1 May 2014

OCA — Thu, 01 May 2014 09:31:01 GMT

←Older revision		Revision as of 09:31, 1 May 2014
Line 2:		Line 2:
	<StructureSection load='4pqa' size='340' side='right' caption='[[4pqa]], [[Resolution\|resolution]] 1.78Å' scene=''>		<StructureSection load='4pqa' size='340' side='right' caption='[[4pqa]], [[Resolution\|resolution]] 1.78Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	[[4pqa]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PQA OCA]. <br>	+	<table><tr><td colspan='2'>[[4pqa]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PQA OCA]. <br>
-	<b>[[Ligand\|Ligands:]]</b> <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=X8Z:L-CAPTOPRIL'>X8Z</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>	+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=X8Z:L-CAPTOPRIL'>X8Z</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
-	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>	+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
-	<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pqa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pqa RCSB], [http://www.ebi.ac.uk/pdbsum/4pqa PDBsum]</span><br>	+	<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=4pqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pqa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pqa RCSB], [http://www.ebi.ac.uk/pdbsum/4pqa PDBsum]</span></td></tr>
		+	<table>
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:06, 30 April 2014

OCA — Wed, 30 Apr 2014 10:06:01 GMT

←Older revision		Revision as of 10:06, 30 April 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	[[4pqa]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PQA OCA]. <br>		[[4pqa]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PQA OCA]. <br>
		+	<b>[[Ligand\|Ligands:]]</b> <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=X8Z:L-CAPTOPRIL'>X8Z</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>		<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
		+	<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pqa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pqa RCSB], [http://www.ebi.ac.uk/pdbsum/4pqa PDBsum]</span><br>
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:09, 30 April 2014

OCA — Wed, 30 Apr 2014 08:09:41 GMT

←Older revision		Revision as of 08:09, 30 April 2014
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal Structure of succinyl-diaminopimelate desuccinylase from Neisseria meningitidis MC58 in complex with the Inhibitor Captopril==
-		+	<StructureSection load='4pqa' size='340' side='right' caption='[[4pqa]], [[Resolution\|resolution]] 1.78Å' scene=''>
-	~~The entry~~ 4pqa is ~~ON HOLD~~	+	== Structural highlights ==
-		+	[[4pqa]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PQA OCA]. <br>
-	~~Authors~~: ~~Nocek, B~~.~~, Starus ,A~~., ~~Holz, R~~., Anderson, W.F.~~, Joachimiak, A.~~, Center for Structural Genomics of Infectious Diseases ~~(CSGID)~~	+	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
-		+	== References ==
-	~~Description~~: ~~Crystal Structure~~ of ~~succinyl~~-~~diaminopimelate desuccinylase from Neisseria meningitidis MC58 in~~ complex ~~with the Inhibitor Captopril~~	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Succinyl-diaminopimelate desuccinylase]]
		+	[[Category: Anderson, W F.]]
		+	[[Category: CSGID, Center for Structural Genomics of Infectious Diseases.]]
		+	[[Category: Holz, R.]]
		+	[[Category: Joachimiak, A.]]
		+	[[Category: Nocek, B.]]
		+	[[Category: Starus ,A.]]
		+	[[Category: Captopril]]
		+	[[Category: Center for structural genomics of infectious disease]]
		+	[[Category: Csgid]]
		+	[[Category: Dape]]
		+	[[Category: Hydrolase]]
		+	[[Category: Hydrolase-hydrolase inhibitor complex]]
		+	[[Category: M20 aminopeptidase]]
		+	[[Category: Metaloenzyme]]
		+	[[Category: National institute of allergy and infectious disease]]
		+	[[Category: Niaid]]
		+	[[Category: Structural genomic]]

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

OCA — Wed, 12 Mar 2014 12:35:05 GMT

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

←Older revision

Revision as of 12:35, 12 March 2014

OCA: New page: '''Unreleased structure''' The entry 4pqa is ON HOLD Authors: Nocek, B., Starus ,A., Holz, R., Anderson, W.F., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSG...

OCA — Wed, 12 Mar 2014 12:35:04 GMT

New page: '''Unreleased structure''' The entry 4pqa is ON HOLD Authors: Nocek, B., Starus ,A., Holz, R., Anderson, W.F., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSG...

New page

'''Unreleased structure'''

The entry 4pqa is ON HOLD

Authors: Nocek, B., Starus ,A., Holz, R., Anderson, W.F., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSGID)

Description: Crystal Structure of succinyl-diaminopimelate desuccinylase from Neisseria meningitidis MC58 in complex with the Inhibitor Captopril