3mrt - Revision history

OCA at 08:59, 6 September 2023

2023-09-06T08:59:44Z

← Older revision		Revision as of 08:59, 6 September 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3mrt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MRT FirstGlance]. <br>		<table><tr><td colspan='2'>[[3mrt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MRT FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=12E:N~~-{[~~(2E)-2-(PYRIDIN-4-YLMETHYLIDENE)HYDRAZINO~~]~~CARBONOTHIOYL}-BETA-D-GLUCOPYRANOSYLAMINE'>12E</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]] 1.98Å</td></tr>
	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene~~></td></tr>~~		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=12E:N-{[(2E)-2-(PYRIDIN-4-YLMETHYLIDENE)HYDRAZINO]CARBONOTHIOYL}-BETA-D-GLUCOPYRANOSYLAMINE'>12E</scene>, <scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3mqf\|3mqf]], [[3mrv\|3mrv]], [[3mrx\|3mrx]], [[3ms2\|3ms2]], [[3ms4\|3ms4]], [[3ms7\|3ms7]], [[3msc\|3msc]], [[3mt7\|3mt7]], [[3mt8\|3mt8]], [[3mt9\|3mt9]], [[3mta\|3mta]], [[3mtb\|3mtb]], [[3mtd\|3mtd]]</div></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </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=3mrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mrt OCA], [https://pdbe.org/3mrt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mrt RCSB], [https://www.ebi.ac.uk/pdbsum/3mrt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mrt 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=3mrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mrt OCA], [https://pdbe.org/3mrt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mrt RCSB], [https://www.ebi.ac.uk/pdbsum/3mrt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mrt ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/PYGM_RABIT PYGM_RABIT]] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.		[https://www.uniprot.org/uniprot/PYGM_RABIT PYGM_RABIT] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	~~[[Category: Phosphorylase]]~~		[[Category: Alexacou K-M]]
	[[Category: Alexacou, K M]]
	~~[[Category: Glycogenolysis]]~~
	~~[[Category: Transferase-transferase inhibitor complex]]~~
	~~[[Category: Type 2 diabetes~~]]

OCA at 13:50, 4 May 2022

2022-05-04T13:50:32Z

OCA at 11:21, 17 July 2019

2019-07-17T11:21:09Z

← Older revision		Revision as of 11:21, 17 July 2019
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	==Glycogen phosphorylase complexed with 4-pyridinecarboxaldehyde-4-(beta-D-glucopyranosyl) thiosemicarbazone==		==Glycogen phosphorylase complexed with 4-pyridinecarboxaldehyde-4-(beta-D-glucopyranosyl) thiosemicarbazone==
	<StructureSection load='3mrt' size='340' side='right' caption='[[3mrt]], [[Resolution\|resolution]] 1.98Å' scene=''>		<StructureSection load='3mrt' size='340' side='right'caption='[[3mrt]], [[Resolution\|resolution]] 1.98Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3mrt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MRT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MRT FirstGlance]. <br>		<table><tr><td colspan='2'>[[3mrt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MRT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MRT FirstGlance]. <br>
Line 23:		Line 23:

	==See Also==		==See Also==
	*[[Glycogen ~~Phosphorylase~~\|Glycogen ~~Phosphorylase~~]]		*[[Glycogen phosphorylase 3D structures\|Glycogen phosphorylase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Large Structures]]
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	[[Category: Phosphorylase]]		[[Category: Phosphorylase]]

OCA at 07:13, 4 August 2016

2016-08-04T07:13:51Z

← Older revision		Revision as of 07:13, 4 August 2016
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	==Glycogen phosphorylase complexed with 4-pyridinecarboxaldehyde-4-(beta-D-glucopyranosyl) thiosemicarbazone==		==Glycogen phosphorylase complexed with 4-pyridinecarboxaldehyde-4-(beta-D-glucopyranosyl) thiosemicarbazone==
	<StructureSection load='3mrt' size='340' side='right' caption='[[3mrt]], [[Resolution\|resolution]] 1.98Å' scene=''>		<StructureSection load='3mrt' size='340' side='right' caption='[[3mrt]], [[Resolution\|resolution]] 1.98Å' scene=''>
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	<table><tr><td colspan='2'>[[3mrt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MRT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MRT FirstGlance]. <br>		<table><tr><td colspan='2'>[[3mrt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MRT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MRT FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=12E:N-{[(2E)-2-(PYRIDIN-4-YLMETHYLIDENE)HYDRAZINO]CARBONOTHIOYL}-BETA-D-GLUCOPYRANOSYLAMINE'>12E</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=12E:N-{[(2E)-2-(PYRIDIN-4-YLMETHYLIDENE)HYDRAZINO]CARBONOTHIOYL}-BETA-D-GLUCOPYRANOSYLAMINE'>12E</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-~~LYSINE(~~3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-~~YLMETHANE)~~'>LLP</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3mqf\|3mqf]], [[3mrv\|3mrv]], [[3mrx\|3mrx]], [[3ms2\|3ms2]], [[3ms4\|3ms4]], [[3ms7\|3ms7]], [[3msc\|3msc]], [[3mt7\|3mt7]], [[3mt8\|3mt8]], [[3mt9\|3mt9]], [[3mta\|3mta]], [[3mtb\|3mtb]], [[3mtd\|3mtd]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3mqf\|3mqf]], [[3mrv\|3mrv]], [[3mrx\|3mrx]], [[3ms2\|3ms2]], [[3ms4\|3ms4]], [[3ms7\|3ms7]], [[3msc\|3msc]], [[3mt7\|3mt7]], [[3mt8\|3mt8]], [[3mt9\|3mt9]], [[3mta\|3mta]], [[3mtb\|3mtb]], [[3mtd\|3mtd]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </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=3mrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mrt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mrt RCSB], [http://www.ebi.ac.uk/pdbsum/3mrt 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=3mrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mrt OCA], [http://pdbe.org/3mrt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mrt RCSB], [http://www.ebi.ac.uk/pdbsum/3mrt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mrt ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 3mrt" style="background-color:#fffaf0;"></div>

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

OCA at 06:34, 24 December 2014

2014-12-24T06:34:18Z

← Older revision		Revision as of 06:34, 24 December 2014
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	<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=3mrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mrt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mrt RCSB], [http://www.ebi.ac.uk/pdbsum/3mrt 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=3mrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mrt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mrt RCSB], [http://www.ebi.ac.uk/pdbsum/3mrt PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/PYGM_RABIT PYGM_RABIT]] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 08:24, 9 December 2014

2014-12-09T08:24:06Z

← Older revision		Revision as of 08:24, 9 December 2014
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	[[~~Image~~:~~3mrt~~.~~png~~\|~~left~~\|~~200px~~]]		==Glycogen phosphorylase complexed with 4-pyridinecarboxaldehyde-4-(beta-D-glucopyranosyl) thiosemicarbazone==
			<StructureSection load='3mrt' size='340' side='right' caption='[[3mrt]], [[Resolution\|resolution]] 1.98Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[3mrt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MRT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MRT FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=12E:N-{[(2E)-2-(PYRIDIN-4-YLMETHYLIDENE)HYDRAZINO]CARBONOTHIOYL}-BETA-D-GLUCOPYRANOSYLAMINE'>12E</scene></td></tr>
			<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3mqf\|3mqf]], [[3mrv\|3mrv]], [[3mrx\|3mrx]], [[3ms2\|3ms2]], [[3ms4\|3ms4]], [[3ms7\|3ms7]], [[3msc\|3msc]], [[3mt7\|3mt7]], [[3mt8\|3mt8]], [[3mt9\|3mt9]], [[3mta\|3mta]], [[3mtb\|3mtb]], [[3mtd\|3mtd]]</td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </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=3mrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mrt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mrt RCSB], [http://www.ebi.ac.uk/pdbsum/3mrt PDBsum]</span></td></tr>
			</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Glycogen phosphorylase (GP) is a promising target for the treatment of type 2 diabetes. In the process of structure based drug design for GP, a group of 15 aromatic aldehyde 4-(beta-d-glucopyranosyl)thiosemicarbazones have been synthesized and evaluated as inhibitors of rabbit muscle glycogen phosphorylase b (GPb) by kinetic studies. These compounds are competitive inhibitors of GPb with respect to alpha-d-glucose-1-phosphate with IC(50) values ranging from 5.7 to 524.3muM. In order to elucidate the structural basis of their inhibition, the crystal structures of these compounds in complex with GPb at 1.95-2.23A resolution were determined. The complex structures reveal that the inhibitors are accommodated at the catalytic site with the glucopyranosyl moiety at approximately the same position as alpha-d-glucose and stabilize the T conformation of the 280s loop. The thiosemicarbazone part of the studied glucosyl thiosemicarbazones possess a moiety derived from substituted benzaldehydes with NO(2), F, Cl, Br, OH, OMe, CF(3), or Me at the ortho-, meta- or para-position of the aromatic ring as well as a moiety derived from 4-pyridinecarboxaldehyde. These fit tightly into the beta-pocket, a side channel from the catalytic site with no access to the bulk solvent. The differences in their inhibitory potency can be interpreted in terms of variations in the interactions of the aldehyde-derived moiety with protein residues in the beta-pocket. In addition, 14 out of the 15 studied inhibitors were found bound at the new allosteric site of the enzyme.

	~~{{STRUCTURE_3mrt\| PDB=3mrt \| SCENE= }}~~		The binding of beta-d-glucopyranosyl-thiosemicarbazone derivatives to glycogen phosphorylase: A new class of inhibitors.,Alexacou KM, Tenchiu Deleanu AC, Chrysina ED, Charavgi MD, Kostas ID, Zographos SE, Oikonomakos NG, Leonidas DD Bioorg Med Chem. 2010 Nov 15;18(22):7911-22. Epub 2010 Sep 22. PMID:20947361<ref>PMID:20947361</ref>

	~~===Glycogen phosphorylase complexed with 4-pyridinecarboxaldehyde-4-(beta-D-glucopyranosyl) thiosemicarbazone===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_20947361}}~~

	~~==About this Structure==~~
	~~[[3mrt]] is~~ a ~~1 chain structure with sequence from [http://en.wikipedia~~.~~org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann.ac.il/oca-bin~~/~~ocashort?id=3MRT OCA].~~

	==See Also==		==See Also==
	*[[Glycogen Phosphorylase\|Glycogen Phosphorylase]]		*[[Glycogen Phosphorylase\|Glycogen Phosphorylase]]
			== References ==
	==~~Reference~~==		<references/>
	<~~ref group="xtra">PMID:020947361<~~/~~ref~~><~~references group="xtra"~~/>		__TOC__
			</StructureSection>
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	[[Category: Phosphorylase]]		[[Category: Phosphorylase]]
	[[Category: Alexacou, K M.]]		[[Category: Alexacou, K M]]
	[[Category: Glycogenolysis]]		[[Category: Glycogenolysis]]
	[[Category: Transferase-transferase inhibitor complex]]		[[Category: Transferase-transferase inhibitor complex]]
	[[Category: Type 2 diabetes]]		[[Category: Type 2 diabetes]]

OCA at 05:14, 20 October 2012

2012-10-20T05:14:25Z

← Older revision		Revision as of 05:14, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
	[[3mrt]] is a 1 chain structure ~~of [[Glycogen Phosphorylase]]~~ with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MRT OCA].		[[3mrt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MRT OCA].

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

OCA at 09:25, 25 July 2012

2012-07-25T09:25:39Z

← Older revision		Revision as of 09:25, 25 July 2012
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	[[Image:3mrt.~~jpg~~\|left\|200px]]		[[Image:3mrt.png\|left\|200px]]

	~~<!--~~
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	{{STRUCTURE_3mrt\| PDB=3mrt \| SCENE= }}		{{STRUCTURE_3mrt\| PDB=3mrt \| SCENE= }}

	===Glycogen phosphorylase complexed with 4-pyridinecarboxaldehyde-4-(beta-D-glucopyranosyl) thiosemicarbazone===		===Glycogen phosphorylase complexed with 4-pyridinecarboxaldehyde-4-(beta-D-glucopyranosyl) thiosemicarbazone===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_20947361}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 20947361 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_20947361}}		{{ABSTRACT_PUBMED_20947361}}

	==About this Structure==		==About this Structure==
	[[3mrt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MRT OCA].		[[3mrt]] is a 1 chain structure of [[Glycogen Phosphorylase]] with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MRT OCA].

			==See Also==
			*[[Glycogen Phosphorylase\|Glycogen Phosphorylase]]

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~20947361~~</ref><references group="xtra"/>		<ref group="xtra">PMID:020947361</ref><references group="xtra"/>
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	[[Category: Phosphorylase]]		[[Category: Phosphorylase]]
	[[Category: Alexacou, K M.]]		[[Category: Alexacou, K M.]]
			[[Category: Glycogenolysis]]
			[[Category: Transferase-transferase inhibitor complex]]
			[[Category: Type 2 diabetes]]

OCA: Protected "3mrt" [edit=sysop:move=sysop]

2011-01-05T16:24:13Z

Protected "3mrt" [edit=sysop:move=sysop]

← Older revision	Revision as of 16:24, 5 January 2011
(No difference)

OCA at 16:24, 5 January 2011

2011-01-05T16:24:12Z

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-'''Unreleased structure'''
+[[Image:3mrt.jpg|left|200px]]
-The entry 3mrt is ON HOLD  until Paper Publication
+<!--
-Authors: Alexacou, K.-M.
+===Glycogen phosphorylase complexed with 4-pyridinecarboxaldehyde-4-(beta-D-glucopyranosyl) thiosemicarbazone===
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug  4 08:46:15 2010''
+<!--

← Older revision		Revision as of 13:50, 4 May 2022
Line 3:		Line 3:
	<StructureSection load='3mrt' size='340' side='right'caption='[[3mrt]], [[Resolution\|resolution]] 1.98Å' scene=''>		<StructureSection load='3mrt' size='340' side='right'caption='[[3mrt]], [[Resolution\|resolution]] 1.98Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3mrt]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MRT OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3MRT FirstGlance]. <br>		<table><tr><td colspan='2'>[[3mrt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MRT FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=12E:N-{[(2E)-2-(PYRIDIN-4-YLMETHYLIDENE)HYDRAZINO]CARBONOTHIOYL}-BETA-D-GLUCOPYRANOSYLAMINE'>12E</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=12E:N-{[(2E)-2-(PYRIDIN-4-YLMETHYLIDENE)HYDRAZINO]CARBONOTHIOYL}-BETA-D-GLUCOPYRANOSYLAMINE'>12E</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3mqf\|3mqf]], [[3mrv\|3mrv]], [[3mrx\|3mrx]], [[3ms2\|3ms2]], [[3ms4\|3ms4]], [[3ms7\|3ms7]], [[3msc\|3msc]], [[3mt7\|3mt7]], [[3mt8\|3mt8]], [[3mt9\|3mt9]], [[3mta\|3mta]], [[3mtb\|3mtb]], [[3mtd\|3mtd]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3mqf\|3mqf]], [[3mrv\|3mrv]], [[3mrx\|3mrx]], [[3ms2\|3ms2]], [[3ms4\|3ms4]], [[3ms7\|3ms7]], [[3msc\|3msc]], [[3mt7\|3mt7]], [[3mt8\|3mt8]], [[3mt9\|3mt9]], [[3mta\|3mta]], [[3mtb\|3mtb]], [[3mtd\|3mtd]]</div></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </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=3mrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mrt OCA], [~~http~~://pdbe.org/3mrt PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3mrt RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3mrt PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3mrt 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=3mrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mrt OCA], [https://pdbe.org/3mrt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mrt RCSB], [https://www.ebi.ac.uk/pdbsum/3mrt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mrt ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/PYGM_RABIT PYGM_RABIT]] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.		[[https://www.uniprot.org/uniprot/PYGM_RABIT PYGM_RABIT]] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==