4ome - Revision history

OCA at 07:32, 25 January 2023

2023-01-25T07:32:31Z

←Older revision		Revision as of 07:32, 25 January 2023
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	<StructureSection load='4ome' size='340' side='right'caption='[[4ome]], [[Resolution\|resolution]] 1.79Å' scene=''>		<StructureSection load='4ome' size='340' side='right'caption='[[4ome]], [[Resolution\|resolution]] 1.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ome]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OME OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4OME FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ome]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OME OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OME FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DGQ:(S)-2-(3-((S)-1-CARBOXY-5-(1,2-DICARBA-CLOSO-DODECARBORANYLAMIDO)+PENTYL)UREIDO)PENTANEDIOIC+ACID'>DGQ</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DGQ:(S)-2-(3-((S)-1-CARBOXY-5-(1,2-DICARBA-CLOSO-DODECARBORANYLAMIDO)+PENTYL)UREIDO)PENTANEDIOIC+ACID'>DGQ</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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">FOLH, FOLH1, GIG27, NAALAD1, PSM, PSMA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4ome FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ome OCA], [https://pdbe.org/4ome PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ome RCSB], [https://www.ebi.ac.uk/pdbsum/4ome PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ome 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/Glutamate_carboxypeptidase_II Glutamate carboxypeptidase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.21 3.4.17.21] </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=4ome FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ome OCA], [~~http~~://pdbe.org/4ome PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4ome RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4ome PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4ome ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/FOLH1_HUMAN FOLH1_HUMAN]] Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Isoform PSM-4 and isoform PSM-5 would appear to be physiologically irrelevant. Involved in prostate tumor progression. Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC.	+	[https://www.uniprot.org/uniprot/FOLH1_HUMAN FOLH1_HUMAN] Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Isoform PSM-4 and isoform PSM-5 would appear to be physiologically irrelevant. Involved in prostate tumor progression. Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC.

	==See Also==		==See Also==
-	*[[Carboxypeptidase\|Carboxypeptidase]]	+	*[[Carboxypeptidase 3D structures\|Carboxypeptidase 3D structures]]
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Glutamate carboxypeptidase II]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Barinka, C]]	+	[[Category: Barinka C]]
-	[[Category: Byun, Y]]	+	[[Category: Byun Y]]
-	[[Category: Novakova, Z]]	+	[[Category: Novakova Z]]
-	[[Category: Ptacek, J]]	+	[[Category: Ptacek J]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Hydrolase-hydrolase inhibitor complex]]~~	+
-	~~[[Category: Metallopeptidase~~]]	+

OCA at 07:40, 17 April 2019

2019-04-17T07:40:30Z

←Older revision		Revision as of 07:40, 17 April 2019
Line 1:		Line 1:

	==X-ray structure of human glutamate carboxypeptidase II in complex with DCCBL, a urea based inhibitor with distal carborane moiety==		==X-ray structure of human glutamate carboxypeptidase II in complex with DCCBL, a urea based inhibitor with distal carborane moiety==
-	<StructureSection load='4ome' size='340' side='right' caption='[[4ome]], [[Resolution\|resolution]] 1.79Å' scene=''>	+	<StructureSection load='4ome' size='340' side='right'caption='[[4ome]], [[Resolution\|resolution]] 1.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ome]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OME OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OME FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ome]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OME OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OME FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DGQ:(S)-2-(3-((S)-1-CARBOXY-5-(1,2-DICARBA-CLOSO-DODECARBORANYLAMIDO)+PENTYL)UREIDO)PENTANEDIOIC+ACID'>DGQ</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <~~scene name~~='~~pdbligand~~=~~MAN~~:~~ALPHA-D-MANNOSE'~~>~~MAN~~</~~scene~~></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DGQ:(S)-2-(3-((S)-1-CARBOXY-5-(1,2-DICARBA-CLOSO-DODECARBORANYLAMIDO)+PENTYL)UREIDO)PENTANEDIOIC+ACID'>DGQ</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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">FOLH, FOLH1, GIG27, NAALAD1, PSM, PSMA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_carboxypeptidase_II Glutamate carboxypeptidase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.21 3.4.17.21] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_carboxypeptidase_II Glutamate carboxypeptidase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.21 3.4.17.21] </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=4ome FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ome OCA], [http://pdbe.org/4ome PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ome RCSB], [http://www.ebi.ac.uk/pdbsum/4ome PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ome ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ome FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ome OCA], [http://pdbe.org/4ome PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ome RCSB], [http://www.ebi.ac.uk/pdbsum/4ome PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ome ProSAT]</span></td></tr>
Line 16:		Line 17:
	</StructureSection>		</StructureSection>
	[[Category: Glutamate carboxypeptidase II]]		[[Category: Glutamate carboxypeptidase II]]
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Barinka, C]]		[[Category: Barinka, C]]
	[[Category: Byun, Y]]		[[Category: Byun, Y]]

OCA at 17:05, 2 January 2017

2017-01-02T17:05:41Z

←Older revision		Revision as of 17:05, 2 January 2017
Line 1:		Line 1:
		+
	==X-ray structure of human glutamate carboxypeptidase II in complex with DCCBL, a urea based inhibitor with distal carborane moiety==		==X-ray structure of human glutamate carboxypeptidase II in complex with DCCBL, a urea based inhibitor with distal carborane moiety==
	<StructureSection load='4ome' size='340' side='right' caption='[[4ome]], [[Resolution\|resolution]] 1.79Å' scene=''>		<StructureSection load='4ome' size='340' side='right' caption='[[4ome]], [[Resolution\|resolution]] 1.79Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DGQ:(S)-2-(3-((S)-1-CARBOXY-5-(1,2-DICARBA-CLOSO-DODECARBORANYLAMIDO)+PENTYL)UREIDO)PENTANEDIOIC+ACID'>DGQ</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DGQ:(S)-2-(3-((S)-1-CARBOXY-5-(1,2-DICARBA-CLOSO-DODECARBORANYLAMIDO)+PENTYL)UREIDO)PENTANEDIOIC+ACID'>DGQ</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_carboxypeptidase_II Glutamate carboxypeptidase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.21 3.4.17.21] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_carboxypeptidase_II Glutamate carboxypeptidase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.21 3.4.17.21] </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=4ome FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ome OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ome RCSB], [http://www.ebi.ac.uk/pdbsum/4ome 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=4ome FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ome OCA], [http://pdbe.org/4ome PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ome RCSB], [http://www.ebi.ac.uk/pdbsum/4ome PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ome ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/FOLH1_HUMAN FOLH1_HUMAN]] Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Isoform PSM-4 and isoform PSM-5 would appear to be physiologically irrelevant. Involved in prostate tumor progression. Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC.		[[http://www.uniprot.org/uniprot/FOLH1_HUMAN FOLH1_HUMAN]] Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Isoform PSM-4 and isoform PSM-5 would appear to be physiologically irrelevant. Involved in prostate tumor progression. Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC.
		+
		+	==See Also==
		+	*[[Carboxypeptidase\|Carboxypeptidase]]
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 13:06, 18 February 2015

2015-02-18T13:06:01Z

←Older revision		Revision as of 13:06, 18 February 2015
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==X-ray structure of human glutamate carboxypeptidase II in complex with DCCBL, a urea based inhibitor with distal carborane moiety==
-		+	<StructureSection load='4ome' size='340' side='right' caption='[[4ome]], [[Resolution\|resolution]] 1.79Å' scene=''>
-	~~The entry~~ 4ome is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4ome]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OME OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OME FirstGlance]. <br>
-	~~Authors~~: ~~Barinka~~, C., ~~Ptacek~~, J., ~~Novakova~~, Z., ~~Byun~~, Y.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DGQ:(S)-2-(3-((S)-1-CARBOXY-5-(1,2-DICARBA-CLOSO-DODECARBORANYLAMIDO)+PENTYL)UREIDO)PENTANEDIOIC+ACID'>DGQ</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
-		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_carboxypeptidase_II Glutamate carboxypeptidase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.21 3.4.17.21] </span></td></tr>
-	~~Description~~: X-~~ray structure~~ of ~~human~~ glutamate ~~carboxypeptidase II~~ in ~~complex with DCCBL,~~ a ~~urea based inhibitor with distal carborane moiety~~	+	<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=4ome FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ome OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ome RCSB], [http://www.ebi.ac.uk/pdbsum/4ome PDBsum]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FOLH1_HUMAN FOLH1_HUMAN]] Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Isoform PSM-4 and isoform PSM-5 would appear to be physiologically irrelevant. Involved in prostate tumor progression. Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC.
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Glutamate carboxypeptidase II]]
	[[Category: Barinka, C]]		[[Category: Barinka, C]]
-	[[Category: Ptacek, J]]
	[[Category: Byun, Y]]		[[Category: Byun, Y]]
	[[Category: Novakova, Z]]		[[Category: Novakova, Z]]
		+	[[Category: Ptacek, J]]
		+	[[Category: Hydrolase]]
		+	[[Category: Hydrolase-hydrolase inhibitor complex]]
		+	[[Category: Metallopeptidase]]

OCA at 07:28, 12 February 2015

2015-02-12T07:28:08Z

←Older revision		Revision as of 07:28, 12 February 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Barinka, C., Ptacek, J., Novakova, Z., Byun, Y.		Authors: Barinka, C., Ptacek, J., Novakova, Z., Byun, Y.

OCA at 12:09, 28 January 2015

2015-01-28T12:09:46Z

←Older revision		Revision as of 12:09, 28 January 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4ome is ON HOLD ~~until Paper Publication~~	+	The entry 4ome is ON HOLD

	Authors: Barinka, C., Ptacek, J., Novakova, Z., Byun, Y.		Authors: Barinka, C., Ptacek, J., Novakova, Z., Byun, Y.

OCA at 14:27, 24 December 2014

2014-12-24T14:27:53Z

←Older revision		Revision as of 14:27, 24 December 2014
Line 6:		Line 6:

	Description: X-ray structure of human glutamate carboxypeptidase II in complex with DCCBL, a urea based inhibitor with distal carborane moiety		Description: X-ray structure of human glutamate carboxypeptidase II in complex with DCCBL, a urea based inhibitor with distal carborane moiety
		+	[[Category: Unreleased Structures]]
		+	[[Category: Barinka, C]]
		+	[[Category: Ptacek, J]]
		+	[[Category: Byun, Y]]
		+	[[Category: Novakova, Z]]

OCA at 07:19, 23 April 2014

2014-04-23T07:19:08Z

←Older revision		Revision as of 07:19, 23 April 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Barinka, C., Ptacek, J., Novakova, Z., Byun, Y.		Authors: Barinka, C., Ptacek, J., Novakova, Z., Byun, Y.

	Description: X-ray structure of human glutamate carboxypeptidase II in complex with DCCBL, a urea based inhibitor with distal carborane moiety		Description: X-ray structure of human glutamate carboxypeptidase II in complex with DCCBL, a urea based inhibitor with distal carborane moiety

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

2014-02-05T10:33:00Z

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

←Older revision

Revision as of 10:33, 5 February 2014

OCA: New page: '''Unreleased structure''' The entry 4ome is ON HOLD Authors: Barinka, C., Ptacek, J., Novakova, Z., Byun, Y. Description: X-ray structure of human glutamate carboxypeptidase II in com...

2014-02-05T10:32:58Z

New page: '''Unreleased structure''' The entry 4ome is ON HOLD Authors: Barinka, C., Ptacek, J., Novakova, Z., Byun, Y. Description: X-ray structure of human glutamate carboxypeptidase II in com...

New page

'''Unreleased structure'''

The entry 4ome is ON HOLD

Authors: Barinka, C., Ptacek, J., Novakova, Z., Byun, Y.

Description: X-ray structure of human glutamate carboxypeptidase II in complex with DCCBL, a urea based inhibitor with distal carborane moiety