4ccd - Revision history

OCA at 12:07, 20 December 2023

2023-12-20T12:07:40Z

← Older revision		Revision as of 12:07, 20 December 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ccd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CCD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CCD FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ccd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CCD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CCD FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2DG:2-DEOXY-BETA-D-GALACTOSE'>2DG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 1.97Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2DG:2-DEOXY-BETA-D-GALACTOSE'>2DG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=4ccd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ccd OCA], [https://pdbe.org/4ccd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ccd RCSB], [https://www.ebi.ac.uk/pdbsum/4ccd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ccd 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=4ccd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ccd OCA], [https://pdbe.org/4ccd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ccd RCSB], [https://www.ebi.ac.uk/pdbsum/4ccd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ccd ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[https://www.uniprot.org/uniprot/GALC_MOUSE GALC_MOUSE]] Defects in Galc are the cause of the 'twitcher' phenotype; an autosomal recessive leukodystrophy similar to the human disease (Krabbe disease). This deficiency results in the insufficient catabolism of several galactolipids that are important in the production of normal myelin.		[https://www.uniprot.org/uniprot/GALC_MOUSE GALC_MOUSE] Defects in Galc are the cause of the 'twitcher' phenotype; an autosomal recessive leukodystrophy similar to the human disease (Krabbe disease). This deficiency results in the insufficient catabolism of several galactolipids that are important in the production of normal myelin.
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/GALC_MOUSE GALC_MOUSE]] Hydrolyzes the galactose ester bonds of galactosylceramide, galactosylsphingosine, lactosylceramide, and monogalactosyldiglyceride. Enzyme with very low activity responsible for the lysosomal catabolism of galactosylceramide, a major lipid in myelin, kidney and epithelial cells of small intestine and colon.<ref>PMID:8769874</ref>		[https://www.uniprot.org/uniprot/GALC_MOUSE GALC_MOUSE] Hydrolyzes the galactose ester bonds of galactosylceramide, galactosylsphingosine, lactosylceramide, and monogalactosyldiglyceride. Enzyme with very low activity responsible for the lysosomal catabolism of galactosylceramide, a major lipid in myelin, kidney and epithelial cells of small intestine and colon.<ref>PMID:8769874</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Glycosphingolipids are ubiquitous components of mammalian cell membranes, and defects in their catabolism by lysosomal enzymes cause a diverse array of diseases. Deficiencies in the enzyme beta-galactocerebrosidase (GALC) cause Krabbe disease, a devastating genetic disorder characterized by widespread demyelination and rapid, fatal neurodegeneration. Here, we present a series of high-resolution crystal structures that illustrate key steps in the catalytic cycle of GALC. We have captured a snapshot of the short-lived enzyme-substrate complex illustrating how wild-type GALC binds a bona fide substrate. We have extensively characterized the enzyme kinetics of GALC with this substrate and shown that the enzyme is active in crystallo by determining the structure of the enzyme-product complex following extended soaking of the crystals with this same substrate. We have also determined the structure of a covalent intermediate that, together with the enzyme-substrate and enzyme-product complexes, reveals conformational changes accompanying the catalytic steps and provides key mechanistic insights, laying the foundation for future design of pharmacological chaperones.

			Structural snapshots illustrate the catalytic cycle of beta-galactocerebrosidase, the defective enzyme in Krabbe disease.,Hill CH, Graham SC, Read RJ, Deane JE Proc Natl Acad Sci U S A. 2013 Dec 2. PMID:24297913<ref>PMID:24297913</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 4ccd" style="background-color:#fffaf0;"></div>

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

OCA at 17:39, 7 September 2022

2022-09-07T17:39:11Z

← Older revision		Revision as of 17:39, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4ccd' size='340' side='right'caption='[[4ccd]], [[Resolution\|resolution]] 1.97Å' scene=''>		<StructureSection load='4ccd' size='340' side='right'caption='[[4ccd]], [[Resolution\|resolution]] 1.97Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ccd]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CCD OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4CCD FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ccd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CCD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CCD FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2DG:2-DEOXY-BETA-D-GALACTOSE'>2DG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene~~></td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2DG:2-DEOXY-BETA-D-GALACTOSE'>2DG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ccc\|4ccc]], [[4cce\|4cce]]</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=4ccd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ccd OCA], [https://pdbe.org/4ccd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ccd RCSB], [https://www.ebi.ac.uk/pdbsum/4ccd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ccd 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/Galactosylceramidase Galactosylceramidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.46 3.2.1.46] </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=4ccd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ccd OCA], [~~http~~://pdbe.org/4ccd PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4ccd RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4ccd PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4ccd ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[~~http~~://www.uniprot.org/uniprot/GALC_MOUSE GALC_MOUSE]] Defects in Galc are the cause of the 'twitcher' phenotype; an autosomal recessive leukodystrophy similar to the human disease (Krabbe disease). This deficiency results in the insufficient catabolism of several galactolipids that are important in the production of normal myelin.		[[https://www.uniprot.org/uniprot/GALC_MOUSE GALC_MOUSE]] Defects in Galc are the cause of the 'twitcher' phenotype; an autosomal recessive leukodystrophy similar to the human disease (Krabbe disease). This deficiency results in the insufficient catabolism of several galactolipids that are important in the production of normal myelin.
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/GALC_MOUSE GALC_MOUSE]] Hydrolyzes the galactose ester bonds of galactosylceramide, galactosylsphingosine, lactosylceramide, and monogalactosyldiglyceride. Enzyme with very low activity responsible for the lysosomal catabolism of galactosylceramide, a major lipid in myelin, kidney and epithelial cells of small intestine and colon.<ref>PMID:8769874</ref>		[[https://www.uniprot.org/uniprot/GALC_MOUSE GALC_MOUSE]] Hydrolyzes the galactose ester bonds of galactosylceramide, galactosylsphingosine, lactosylceramide, and monogalactosyldiglyceride. Enzyme with very low activity responsible for the lysosomal catabolism of galactosylceramide, a major lipid in myelin, kidney and epithelial cells of small intestine and colon.<ref>PMID:8769874</ref>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Glycosphingolipids are ubiquitous components of mammalian cell membranes, and defects in their catabolism by lysosomal enzymes cause a diverse array of diseases. Deficiencies in the enzyme beta-galactocerebrosidase (GALC) cause Krabbe disease, a devastating genetic disorder characterized by widespread demyelination and rapid, fatal neurodegeneration. Here, we present a series of high-resolution crystal structures that illustrate key steps in the catalytic cycle of GALC. We have captured a snapshot of the short-lived enzyme-substrate complex illustrating how wild-type GALC binds a bona fide substrate. We have extensively characterized the enzyme kinetics of GALC with this substrate and shown that the enzyme is active in crystallo by determining the structure of the enzyme-product complex following extended soaking of the crystals with this same substrate. We have also determined the structure of a covalent intermediate that, together with the enzyme-substrate and enzyme-product complexes, reveals conformational changes accompanying the catalytic steps and provides key mechanistic insights, laying the foundation for future design of pharmacological chaperones.

	Structural snapshots illustrate the catalytic cycle of beta-galactocerebrosidase, the defective enzyme in Krabbe disease.,Hill CH, Graham SC, Read RJ, Deane JE Proc Natl Acad Sci U S A. 2013 Dec 2. PMID:24297913<ref>PMID:24297913</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4ccd" style="background-color:#fffaf0;"></div~~>

	==See Also==		==See Also==
Line 29:		Line 18:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	~~[[Category: Galactosylceramidase]]~~
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Lk3 transgenic mice~~]]		[[Category: Mus musculus]]
	[[Category: Deane~~, J E~~]]		[[Category: Deane JE]]
	[[Category: Graham~~, S C~~]]		[[Category: Graham SC]]
	[[Category: Hill~~, C H~~]]		[[Category: Hill CH]]
	[[Category: Read~~, R J]]~~		[[Category: Read RJ]]
	~~[[Category: D-galactal]]~~
	~~[[Category: Enzyme-intermediate complex]]~~
	~~[[Category: Galactosidase]]~~
	~~[[Category: Glycosyl hydrolase]]~~
	~~[[Category: Hydrolase]]~~
	~~[[Category: Krabbe disease]]~~
	~~[[Category: Lysosomal storage disease~~]]

OCA at 09:38, 20 March 2019

2019-03-20T09:38:35Z

← Older revision		Revision as of 09:38, 20 March 2019
Line 1:		Line 1:

	==STRUCTURE OF MOUSE GALACTOCEREBROSIDASE WITH D-GALACTAL: ENZYME- INTERMEDIATE COMPLEX==		==STRUCTURE OF MOUSE GALACTOCEREBROSIDASE WITH D-GALACTAL: ENZYME- INTERMEDIATE COMPLEX==
	<StructureSection load='4ccd' size='340' side='right' caption='[[4ccd]], [[Resolution\|resolution]] 1.97Å' scene=''>		<StructureSection load='4ccd' size='340' side='right'caption='[[4ccd]], [[Resolution\|resolution]] 1.97Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ccd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CCD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CCD FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ccd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CCD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CCD FirstGlance]. <br>
Line 30:		Line 30:
	</StructureSection>		</StructureSection>
	[[Category: Galactosylceramidase]]		[[Category: Galactosylceramidase]]
			[[Category: Large Structures]]
	[[Category: Lk3 transgenic mice]]		[[Category: Lk3 transgenic mice]]
	[[Category: Deane, J E]]		[[Category: Deane, J E]]

OCA at 19:09, 5 August 2016

2016-08-05T19:09:15Z

← Older revision		Revision as of 19:09, 5 August 2016
Line 1:		Line 1:
	~~{{STRUCTURE_4ccd\| PDB=4ccd \| SCENE= }}~~
	~~===STRUCTURE OF MOUSE GALACTOCEREBROSIDASE WITH D-GALACTAL: ENZYME- INTERMEDIATE COMPLEX===~~
	~~{{ABSTRACT_PUBMED_24297913}}~~

	==Disease==		==STRUCTURE OF MOUSE GALACTOCEREBROSIDASE WITH D-GALACTAL: ENZYME- INTERMEDIATE COMPLEX==
			<StructureSection load='4ccd' size='340' side='right' caption='[[4ccd]], [[Resolution\|resolution]] 1.97Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[4ccd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CCD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CCD FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2DG:2-DEOXY-BETA-D-GALACTOSE'>2DG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ccc\|4ccc]], [[4cce\|4cce]]</td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Galactosylceramidase Galactosylceramidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.46 3.2.1.46] </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=4ccd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ccd OCA], [http://pdbe.org/4ccd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ccd RCSB], [http://www.ebi.ac.uk/pdbsum/4ccd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ccd ProSAT]</span></td></tr>
			</table>
			== Disease ==
	[[http://www.uniprot.org/uniprot/GALC_MOUSE GALC_MOUSE]] Defects in Galc are the cause of the 'twitcher' phenotype; an autosomal recessive leukodystrophy similar to the human disease (Krabbe disease). This deficiency results in the insufficient catabolism of several galactolipids that are important in the production of normal myelin.		[[http://www.uniprot.org/uniprot/GALC_MOUSE GALC_MOUSE]] Defects in Galc are the cause of the 'twitcher' phenotype; an autosomal recessive leukodystrophy similar to the human disease (Krabbe disease). This deficiency results in the insufficient catabolism of several galactolipids that are important in the production of normal myelin.
			== Function ==
			[[http://www.uniprot.org/uniprot/GALC_MOUSE GALC_MOUSE]] Hydrolyzes the galactose ester bonds of galactosylceramide, galactosylsphingosine, lactosylceramide, and monogalactosyldiglyceride. Enzyme with very low activity responsible for the lysosomal catabolism of galactosylceramide, a major lipid in myelin, kidney and epithelial cells of small intestine and colon.<ref>PMID:8769874</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Glycosphingolipids are ubiquitous components of mammalian cell membranes, and defects in their catabolism by lysosomal enzymes cause a diverse array of diseases. Deficiencies in the enzyme beta-galactocerebrosidase (GALC) cause Krabbe disease, a devastating genetic disorder characterized by widespread demyelination and rapid, fatal neurodegeneration. Here, we present a series of high-resolution crystal structures that illustrate key steps in the catalytic cycle of GALC. We have captured a snapshot of the short-lived enzyme-substrate complex illustrating how wild-type GALC binds a bona fide substrate. We have extensively characterized the enzyme kinetics of GALC with this substrate and shown that the enzyme is active in crystallo by determining the structure of the enzyme-product complex following extended soaking of the crystals with this same substrate. We have also determined the structure of a covalent intermediate that, together with the enzyme-substrate and enzyme-product complexes, reveals conformational changes accompanying the catalytic steps and provides key mechanistic insights, laying the foundation for future design of pharmacological chaperones.

	~~==Function==~~		Structural snapshots illustrate the catalytic cycle of beta-galactocerebrosidase, the defective enzyme in Krabbe disease.,Hill CH, Graham SC, Read RJ, Deane JE Proc Natl Acad Sci U S A. 2013 Dec 2. PMID:24297913<ref>PMID:24297913</ref>
	~~[[http://www.uniprot.org/uniprot/GALC_MOUSE GALC_MOUSE]] Hydrolyzes~~ the ~~galactose ester bonds~~ of ~~galactosylceramide~~, ~~galactosylsphingosine~~, ~~lactosylceramide~~, ~~and monogalactosyldiglyceride. Enzyme with very low activity responsible for the lysosomal catabolism of galactosylceramide~~, ~~a major lipid in myelin~~, ~~kidney and epithelial cells of small intestine and colon~~.<ref>PMID:~~8769874~~</ref>

	~~==About this Structure==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[4ccd]] is~~ a ~~1 chain structure. Full crystallographic information is available from [http://oca~~.~~weizmann~~.ac.il/~~oca~~-~~bin~~/~~ocashort?id=4CCD OCA].~~		</div>
			<div class="pdbe-citations 4ccd" style="background-color:#fffaf0;"></div>

	==~~Reference~~==		==See Also==
	~~<ref group~~=~~"xtra">PMID:024297913</ref>~~<references ~~group="xtra"~~/><~~references~~/>		*[[Galactosylceramidase\|Galactosylceramidase]]
			== References ==
			<references/>
			__TOC__
			</StructureSection>
	[[Category: Galactosylceramidase]]		[[Category: Galactosylceramidase]]
	[[Category: Deane, J E.]]		[[Category: Lk3 transgenic mice]]
	[[Category: Graham, S C.]]		[[Category: Deane, J E]]
	[[Category: Hill, C H.]]		[[Category: Graham, S C]]
	[[Category: Read, R J.]]		[[Category: Hill, C H]]
			[[Category: Read, R J]]
	[[Category: D-galactal]]		[[Category: D-galactal]]
	[[Category: Enzyme-intermediate complex]]		[[Category: Enzyme-intermediate complex]]

OCA at 13:40, 11 December 2013

2013-12-11T13:40:02Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+{{STRUCTURE_4ccd|  PDB=4ccd  |  SCENE=  }}
-The entry 4ccd is ON HOLD  until Paper Publication
+==Disease==
-Authors: Hill, C.H., Graham, S.C., Read, R.J., Deane, J.E.
+==Function==
-Description: STRUCTURE OF MOUSE GALACTOCEREBROSIDASE WITH D-GALACTAL: ENZYME-INTERMEDIATE COMPLEX
+==About this Structure==

OCA at 09:18, 27 November 2013

2013-11-27T09:18:35Z

← Older revision		Revision as of 09:18, 27 November 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4ccd is ON HOLD		The entry 4ccd is ON HOLD until Paper Publication

	Authors: Hill, C.H., Graham, S.C., Read, R.J., Deane, J.E.		Authors: Hill, C.H., Graham, S.C., Read, R.J., Deane, J.E.

	Description: STRUCTURE OF MOUSE GALACTOCEREBROSIDASE WITH D-GALACTAL: ENZYME-INTERMEDIATE COMPLEX		Description: STRUCTURE OF MOUSE GALACTOCEREBROSIDASE WITH D-GALACTAL: ENZYME-INTERMEDIATE COMPLEX

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

2013-11-06T06:41:03Z

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

← Older revision	Revision as of 06:41, 6 November 2013
(No difference)

OCA: New page: '''Unreleased structure''' The entry 4ccd is ON HOLD Authors: Hill, C.H., Graham, S.C., Read, R.J., Deane, J.E. Description: STRUCTURE OF MOUSE GALACTOCEREBROSIDASE WITH D-GALACTAL: EN...

2013-11-06T06:41:03Z

New page: '''Unreleased structure''' The entry 4ccd is ON HOLD Authors: Hill, C.H., Graham, S.C., Read, R.J., Deane, J.E. Description: STRUCTURE OF MOUSE GALACTOCEREBROSIDASE WITH D-GALACTAL: EN...

New page

'''Unreleased structure'''

The entry 4ccd is ON HOLD

Authors: Hill, C.H., Graham, S.C., Read, R.J., Deane, J.E.

Description: STRUCTURE OF MOUSE GALACTOCEREBROSIDASE WITH D-GALACTAL: ENZYME-INTERMEDIATE COMPLEX