5f09 - Revision history

OCA at 08:38, 12 July 2023

2023-07-12T08:38:00Z

←Older revision		Revision as of 08:38, 12 July 2023
Line 3:		Line 3:
	<StructureSection load='5f09' size='340' side='right'caption='[[5f09]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='5f09' size='340' side='right'caption='[[5f09]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5f09]] 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=5F09 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5F09 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5f09]] 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=5F09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F09 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BC8:BETA-CITRYL-L-GLUTAMIC+ACID'>BC8</scene>, <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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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]] 1.85Å</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FOLH1, FOLH, NAALAD1, PSM, PSMA, GIG27 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BC8:BETA-CITRYL-L-GLUTAMIC+ACID'>BC8</scene>, <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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5f09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f09 OCA], [https://pdbe.org/5f09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f09 RCSB], [https://www.ebi.ac.uk/pdbsum/5f09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f09 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=5f09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f09 OCA], [~~http~~://pdbe.org/5f09 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5f09 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5f09 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5f09 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.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 27:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Glutamate carboxypeptidase II]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Konvalinka, J]]	+	[[Category: Konvalinka J]]
-	[[Category: Navratil, M]]	+	[[Category: Navratil M]]
-	[[Category: Pachl, P]]	+	[[Category: Pachl P]]
-	[[Category: Tykvart, J]]	+	[[Category: Tykvart J]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Inactive variant]]~~	+
-	~~[[Category: Metallopeptidase]]~~	+
-	~~[[Category: Substrate~~]]	+

OCA at 07:53, 29 April 2020

2020-04-29T07:53:42Z

←Older revision		Revision as of 07:53, 29 April 2020
Line 1:		Line 1:

	==Structure of inactive GCPII mutant in complex with beta-citryl glutamate==		==Structure of inactive GCPII mutant in complex with beta-citryl glutamate==
-	<StructureSection load='5f09' size='340' side='right' caption='[[5f09]], [[Resolution\|resolution]] 1.85Å' scene=''>	+	<StructureSection load='5f09' size='340' side='right'caption='[[5f09]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5f09]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F09 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5F09 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5f09]] 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=5F09 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5F09 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BC8:BETA-CITRYL-L-GLUTAMIC+ACID'>BC8</scene>, <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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=BC8:BETA-CITRYL-L-GLUTAMIC+ACID'>BC8</scene>, <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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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">FOLH1, FOLH, NAALAD1, PSM, PSMA, GIG27 ([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=5f09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f09 OCA], [http://pdbe.org/5f09 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f09 RCSB], [http://www.ebi.ac.uk/pdbsum/5f09 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f09 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=5f09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f09 OCA], [http://pdbe.org/5f09 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f09 RCSB], [http://www.ebi.ac.uk/pdbsum/5f09 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f09 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 5f09" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5f09" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Carboxypeptidase 3D structures\|Carboxypeptidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 24:		Line 28:
	</StructureSection>		</StructureSection>
	[[Category: Glutamate carboxypeptidase II]]		[[Category: Glutamate carboxypeptidase II]]
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Konvalinka, J]]		[[Category: Konvalinka, J]]
	[[Category: Navratil, M]]		[[Category: Navratil, M]]

OCA at 03:05, 13 July 2016

2016-07-13T03:05:05Z

←Older revision		Revision as of 03:05, 13 July 2016
Line 6:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BC8:BETA-CITRYL-L-GLUTAMIC+ACID'>BC8</scene>, <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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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"><scene name='pdbligand=BC8:BETA-CITRYL-L-GLUTAMIC+ACID'>BC8</scene>, <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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5f09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f09 OCA], [http://pdbe.org/5f09 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f09 RCSB], [http://www.ebi.ac.uk/pdbsum/5f09 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=5f09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f09 OCA], [http://pdbe.org/5f09 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f09 RCSB], [http://www.ebi.ac.uk/pdbsum/5f09 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f09 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 15:37, 1 June 2016

2016-06-01T15:37:12Z

←Older revision		Revision as of 15:37, 1 June 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5f09 is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Structure of inactive GCPII mutant in complex with beta-citryl glutamate==
		+	<StructureSection load='5f09' size='340' side='right' caption='[[5f09]], [[Resolution\|resolution]] 1.85Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5f09]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F09 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F09 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BC8:BETA-CITRYL-L-GLUTAMIC+ACID'>BC8</scene>, <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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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='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=5f09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f09 OCA], [http://pdbe.org/5f09 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f09 RCSB], [http://www.ebi.ac.uk/pdbsum/5f09 PDBsum]</span></td></tr>
		+	</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.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Glutamate carboxypeptidase III (GCPIII) is best known as a homologue of glutamate carboxypeptidase II [GCPII; also known as prostate-specific membrane antigen (PSMA)], a protease involved in neurological disorders and overexpressed in a number of solid cancers. However, mouse GCPIII was recently shown to cleave beta-citrylglutamate (BCG), suggesting that these two closely related enzymes have distinct functions. To develop a tool to dissect, evaluate and quantify the activities of human GCPII and GCPIII, we analyzed the catalytic efficiencies of these enzymes towards three physiological substrates. We observed a high efficiency of BCG cleavage by GCPIII but not GCPII. We also identified a strong modulation of GCPIII enzymatic activity by divalent cations, while we did not observe this effect for GCPII. Additionally, we used X-ray crystallography and computational modelling (quantum and molecular mechanical calculations) to describe the mechanism of BCG binding to the active sites of GCPII and GCPIII, respectively. Finally, we took advantage of the substantial differences in the enzymatic efficiencies of GCPII and GCPIII towards their substrates, using enzymatic assays for specific detection of these proteins in human tissues. Our findings suggest that GCPIII may not act merely as a complementary enzyme to GCPII, and it more likely possesses a specific physiological function related to BCG metabolism in the human body. This article is protected by copyright. All rights reserved.

-	~~Authors:~~ Tykvart, J., Navratil, M., ~~Pachl~~, P., Konvalinka, J.	+	Comparison of human glutamate carboxypeptidases II and III reveals their divergent substrate specificities.,Navratil M, Tykvart J, Schimer J, Pachl P, Navratil V, Rokob TA, Hlouchova K, Rulisek L, Konvalinka J FEBS J. 2016 May 21. doi: 10.1111/febs.13761. PMID:27208881<ref>PMID:27208881</ref>

-	~~Description: Structure~~ of ~~inactive GCPII mutant in complex with beta~~-~~citryl glutamate~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5f09" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Glutamate carboxypeptidase II]]
	[[Category: Konvalinka, J]]		[[Category: Konvalinka, J]]
-	[[Category: Tykvart, J]]
	[[Category: Navratil, M]]		[[Category: Navratil, M]]
	[[Category: Pachl, P]]		[[Category: Pachl, P]]
		+	[[Category: Tykvart, J]]
		+	[[Category: Hydrolase]]
		+	[[Category: Inactive variant]]
		+	[[Category: Metallopeptidase]]
		+	[[Category: Substrate]]

OCA: Protected "5f09" [edit=sysop:move=sysop]

2015-12-09T12:25:24Z

Protected "5f09" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:25, 9 December 2015

OCA: New page: '''Unreleased structure''' The entry 5f09 is ON HOLD until Paper Publication Authors: Tykvart, J., Navratil, M., Pachl, P., Konvalinka, J. Description: Structure of inactive GCPII muta...

2015-12-09T12:25:22Z

New page: '''Unreleased structure''' The entry 5f09 is ON HOLD until Paper Publication Authors: Tykvart, J., Navratil, M., Pachl, P., Konvalinka, J. Description: Structure of inactive GCPII muta...

New page

'''Unreleased structure'''

The entry 5f09 is ON HOLD until Paper Publication

Authors: Tykvart, J., Navratil, M., Pachl, P., Konvalinka, J.

Description: Structure of inactive GCPII mutant in complex with beta-citryl glutamate
[[Category: Unreleased Structures]]
[[Category: Konvalinka, J]]
[[Category: Tykvart, J]]
[[Category: Navratil, M]]
[[Category: Pachl, P]]