3mig - Revision history

OCA at 08:54, 6 September 2023

2023-09-06T08:54:12Z

← Older revision		Revision as of 08:54, 6 September 2023
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	<StructureSection load='3mig' size='340' side='right'caption='[[3mig]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='3mig' size='340' side='right'caption='[[3mig]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3mig]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Buffalo_rat Buffalo rat~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MIG FirstGlance]. <br>		<table><tr><td colspan='2'>[[3mig]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MIG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=NO2:NITRITE+ION'>NO2</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]] 2.7Å</td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1phm\|1phm]], [[3mib\|3mib]], [[3mic\|3mic]], [[3mid\|3mid]], [[3mie\|3mie]], [[3mif\|3mif]], [[3mih\|3mih]], [[3mlj\|3mlj]], [[3mlk\|3mlk]], [[3mll\|3mll]]</div></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=NO2:NITRITE+ION'>NO2</scene></td></tr>
	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Pam ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>~~
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidylglycine_monooxygenase Peptidylglycine monooxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.3 1.14.17.3] </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=3mig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mig OCA], [https://pdbe.org/3mig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mig RCSB], [https://www.ebi.ac.uk/pdbsum/3mig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mig 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=3mig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mig OCA], [https://pdbe.org/3mig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mig RCSB], [https://www.ebi.ac.uk/pdbsum/3mig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mig ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/AMD_RAT AMD_RAT]] Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.		[https://www.uniprot.org/uniprot/AMD_RAT AMD_RAT] Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	~~[[Category: Buffalo rat]]~~
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Peptidylglycine monooxygenase~~]]		[[Category: Rattus norvegicus]]
	[[Category: Amzel~~, L M~~]]		[[Category: Amzel LM]]
	[[Category: Chufan~~, E E~~]]		[[Category: Chufan EE]]
	[[Category: Eipper~~, B A~~]]		[[Category: Eipper BA]]
	[[Category: Mains~~, R E]]~~		[[Category: Mains RE]]
	~~[[Category: Ascorbate]]~~
	~~[[Category: Bioactive peptide activation]]~~
	~~[[Category: Monooxygenase]]~~
	~~[[Category: Oxidoreductase~~]]

OCA at 13:47, 4 May 2022

2022-05-04T13:47:10Z

← Older revision		Revision as of 13:47, 4 May 2022
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	==Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound nitrite, obtained in the presence of substrate==		==Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound nitrite, obtained in the presence of substrate==
	<StructureSection load='3mig' size='340' side='right' caption='[[3mig]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='3mig' size='340' side='right'caption='[[3mig]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3mig]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MIG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3MIG FirstGlance]. <br>		<table><tr><td colspan='2'>[[3mig]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MIG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=NO2:NITRITE+ION'>NO2</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=NO2:NITRITE+ION'>NO2</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1phm\|1phm]], [[3mib\|3mib]], [[3mic\|3mic]], [[3mid\|3mid]], [[3mie\|3mie]], [[3mif\|3mif]], [[3mih\|3mih]], [[3mlj\|3mlj]], [[3mlk\|3mlk]], [[3mll\|3mll]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1phm\|1phm]], [[3mib\|3mib]], [[3mic\|3mic]], [[3mid\|3mid]], [[3mie\|3mie]], [[3mif\|3mif]], [[3mih\|3mih]], [[3mlj\|3mlj]], [[3mlk\|3mlk]], [[3mll\|3mll]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Pam ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Pam ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Peptidylglycine_monooxygenase Peptidylglycine monooxygenase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.3 1.14.17.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidylglycine_monooxygenase Peptidylglycine monooxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.3 1.14.17.3] </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=3mig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mig OCA], [~~http~~://pdbe.org/3mig PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3mig RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3mig PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3mig 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=3mig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mig OCA], [https://pdbe.org/3mig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mig RCSB], [https://www.ebi.ac.uk/pdbsum/3mig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mig ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/AMD_RAT AMD_RAT]] Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.		[[https://www.uniprot.org/uniprot/AMD_RAT AMD_RAT]] Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	==See Also==		==See Also==
	*[[Monooxygenase\|Monooxygenase]]		*[[Monooxygenase 3D structures\|Monooxygenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Buffalo rat]]		[[Category: Buffalo rat]]
			[[Category: Large Structures]]
	[[Category: Peptidylglycine monooxygenase]]		[[Category: Peptidylglycine monooxygenase]]
	[[Category: Amzel, L M]]		[[Category: Amzel, L M]]

OCA at 07:06, 9 January 2019

2019-01-09T07:06:24Z

← Older revision		Revision as of 07:06, 9 January 2019
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	</div>		</div>
	<div class="pdbe-citations 3mig" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3mig" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Monooxygenase\|Monooxygenase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:40, 4 August 2016

2016-08-04T08:40:32Z

← Older revision		Revision as of 08:40, 4 August 2016
Line 1:		Line 1:

	==Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound nitrite, obtained in the presence of substrate==		==Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound nitrite, obtained in the presence of substrate==
	<StructureSection load='3mig' size='340' side='right' caption='[[3mig]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='3mig' size='340' side='right' caption='[[3mig]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3mig]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Rattus_norvegicus Rattus norvegicus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MIG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MIG FirstGlance]. <br>		<table><tr><td colspan='2'>[[3mig]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MIG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MIG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=NO2:NITRITE+ION'>NO2</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=NO2:NITRITE+ION'>NO2</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1phm\|1phm]], [[3mib\|3mib]], [[3mic\|3mic]], [[3mid\|3mid]], [[3mie\|3mie]], [[3mif\|3mif]], [[3mih\|3mih]], [[3mlj\|3mlj]], [[3mlk\|3mlk]], [[3mll\|3mll]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1phm\|1phm]], [[3mib\|3mib]], [[3mic\|3mic]], [[3mid\|3mid]], [[3mie\|3mie]], [[3mif\|3mif]], [[3mih\|3mih]], [[3mlj\|3mlj]], [[3mlk\|3mlk]], [[3mll\|3mll]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Pam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 ~~Rattus norvegicus~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Pam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylglycine_monooxygenase Peptidylglycine monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.3 1.14.17.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylglycine_monooxygenase Peptidylglycine monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.3 1.14.17.3] </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=3mig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mig OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mig RCSB], [http://www.ebi.ac.uk/pdbsum/3mig 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=3mig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mig OCA], [http://pdbe.org/3mig PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mig RCSB], [http://www.ebi.ac.uk/pdbsum/3mig PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mig ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	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 3mig" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Buffalo rat]]
	[[Category: Peptidylglycine monooxygenase]]		[[Category: Peptidylglycine monooxygenase]]
	~~[[Category: Rattus norvegicus]]~~
	[[Category: Amzel, L M]]		[[Category: Amzel, L M]]
	[[Category: Chufan, E E]]		[[Category: Chufan, E E]]

OCA at 07:48, 24 December 2014

2014-12-24T07:48:07Z

← Older revision		Revision as of 07:48, 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=3mig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mig OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mig RCSB], [http://www.ebi.ac.uk/pdbsum/3mig 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=3mig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mig OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mig RCSB], [http://www.ebi.ac.uk/pdbsum/3mig PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/AMD_RAT AMD_RAT]] Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 15:55, 18 December 2014

2014-12-18T15:55:05Z

← Older revision		Revision as of 15:55, 18 December 2014
Line 1:		Line 1:
	~~{{STRUCTURE_3mig\| PDB=3mig \| SCENE= }}~~		==Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound nitrite, obtained in the presence of substrate==
	===Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound nitrite, obtained in the presence of substrate===		<StructureSection load='3mig' size='340' side='right' caption='[[3mig]], [[Resolution\|resolution]] 2.70Å' scene=''>
	~~{{ABSTRACT_PUBMED_20958070}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[3mig]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MIG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MIG FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=NO2:NITRITE+ION'>NO2</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1phm\|1phm]], [[3mib\|3mib]], [[3mic\|3mic]], [[3mid\|3mid]], [[3mie\|3mie]], [[3mif\|3mif]], [[3mih\|3mih]], [[3mlj\|3mlj]], [[3mlk\|3mlk]], [[3mll\|3mll]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Pam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylglycine_monooxygenase Peptidylglycine monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.3 1.14.17.3] </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=3mig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mig OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mig RCSB], [http://www.ebi.ac.uk/pdbsum/3mig PDBsum]</span></td></tr>
			</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Peptidylglycine alpha-hydroxylating monooxygenase (PHM) catalyzes the stereospecific hydroxylation of the Calpha of C-terminal glycine-extended peptides and proteins, the first step in the activation of many peptide hormones, growth factors, and neurotransmitters. The crystal structure of the enzyme revealed two nonequivalent Cu sites (Cu(M) and Cu(H)) separated by approximately 11 A. In the resting state of the enzyme, Cu(M) is coordinated in a distorted tetrahedral geometry by one methionine, two histidines, and a water molecule. The coordination site of the water molecule is the position where external ligands bind. The Cu(H) has a planar T-shaped geometry with three histidines residues and a vacant position that could potentially be occupied by a fourth ligand. Although the catalytic mechanism of PHM and the role of the metals are still being debated, Cu(M) is identified as the metal involved in catalysis, while Cu(H) is associated with electron transfer. To further probe the role of the metals, we studied how small molecules such as nitrite (NO(2)(-)), azide (N(3)(-)), and carbon monoxide (CO) interact with the PHM copper ions. The crystal structure of an oxidized nitrite-soaked PHMcc, obtained by soaking for 20 h in mother liquor supplemented with 300 mM NaNO(2), shows that nitrite anion coordinates Cu(M) in an asymmetric bidentate fashion. Surprisingly, nitrite does not bind Cu(H), despite the high concentration used in the experiments (nitrite/protein > 1000). Similarly, azide and carbon monoxide coordinate Cu(M) but not Cu(H) in the PHMcc crystal structures obtained by cocrystallization with 40 mM NaN(3) and by soaking CO under 3 atm of pressure for 30 min. This lack of reactivity at the Cu(H) is also observed in the reduced form of the enzyme: CO binds Cu(M) but not Cu(H) in the structure of PHMcc obtained by exposure of a crystal to 3 atm CO for 15 min in the presence of 5 mM ascorbic acid (reductant). The necessity of Cu(H) to maintain its redox potential in a narrow range compatible with its role as an electron-transfer site seems to explain the lack of coordination of small molecules to Cu(H); coordination of any external ligand will certainly modify its redox potential.

	~~==Function==~~		Differential reactivity between two copper sites in peptidylglycine alpha-hydroxylating monooxygenase.,Chufan EE, Prigge ST, Siebert X, Eipper BA, Mains RE, Amzel LM J Am Chem Soc. 2010 Nov 10;132(44):15565-72. PMID:20958070<ref>PMID:20958070</ref>
	~~[[http://www.uniprot.org/uniprot/AMD_RAT AMD_RAT]] Bifunctional enzyme that catalyzes 2 sequential steps~~ in ~~C-terminal~~ alpha-~~amidation of peptides~~. ~~The monooxygenase part produces an unstable peptidyl~~(~~2-hydroxyglycine~~) ~~intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C~~-~~terminal amidation of peptides such as neuropeptides is essential for full biological activity~~.

	~~==About this Structure==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[3mig]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Rattus_norvegicus Rattus norvegicus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3MIG OCA].~~		</div>
			== References ==
	==~~Reference~~==		<references/>
	~~<ref group="xtra">PMID:020958070</ref>~~<references ~~group="xtra"~~/><~~references~~/>		__TOC__
			</StructureSection>
	[[Category: Peptidylglycine monooxygenase]]		[[Category: Peptidylglycine monooxygenase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
	[[Category: Amzel, L M.]]		[[Category: Amzel, L M]]
	[[Category: Chufan, E E.]]		[[Category: Chufan, E E]]
	[[Category: Eipper, B A.]]		[[Category: Eipper, B A]]
	[[Category: Mains, R E.]]		[[Category: Mains, R E]]
	[[Category: Ascorbate]]		[[Category: Ascorbate]]
	[[Category: Bioactive peptide activation]]		[[Category: Bioactive peptide activation]]
	[[Category: Monooxygenase]]		[[Category: Monooxygenase]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

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

2013-04-17T20:56:34Z

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

← Older revision	Revision as of 20:56, 17 April 2013
(No difference)

OCA at 20:56, 17 April 2013

2013-04-17T20:56:31Z

← Older revision		Revision as of 20:56, 17 April 2013
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	~~{{Seed}}~~
	~~[[Image:3mig.jpg\|left\|200px]]~~

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_3mig", creates the "Structure Box" on the page.~~
	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~
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	{{STRUCTURE_3mig\| PDB=3mig \| SCENE= }}		{{STRUCTURE_3mig\| PDB=3mig \| SCENE= }}

	===Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound nitrite, obtained in the presence of substrate===		===Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound nitrite, obtained in the presence of substrate===
			{{ABSTRACT_PUBMED_20958070}}

			==Function==
	~~<!--~~		[[http://www.uniprot.org/uniprot/AMD_RAT AMD_RAT]] Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
	~~The line below this paragraph, {{ABSTRACT_PUBMED_20958070}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at~~ http://www.~~pubmed~~.~~gov~~)~~, where 20958070~~ is the ~~PubMed ID number~~.
	-->
	~~{{ABSTRACT_PUBMED_20958070}}~~

	==About this Structure==		==About this Structure==
	~~3MIG~~ is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MIG OCA].		[[3mig]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MIG OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~20958070~~</ref><references group="xtra"/>		<ref group="xtra">PMID:020958070</ref><references group="xtra"/><references/>
	[[Category: Peptidylglycine monooxygenase]]		[[Category: Peptidylglycine monooxygenase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
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	[[Category: Monooxygenase]]		[[Category: Monooxygenase]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 24 14:15:09 2010''~~

OCA at 11:03, 24 November 2010

2010-11-24T11:03:39Z

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-'''Unreleased structure'''
+{{Seed}}
-The entry 3mig is ON HOLD  until Paper Publication
+<!--
-Authors: Chufan, E.E., Eipper, B.A., Mains, R.E., Amzel, L.M.
+===Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound nitrite, obtained in the presence of substrate===
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 12 10:45:51 2010''
+<!--

OCA at 07:45, 12 May 2010

2010-05-12T07:45:51Z

← Older revision		Revision as of 07:45, 12 May 2010
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 3mig is ON HOLD		The entry 3mig is ON HOLD until Paper Publication

	Authors: Chufan, E.E., Eipper, B.A., Mains, R.E., Amzel, L.M.		Authors: Chufan, E.E., Eipper, B.A., Mains, R.E., Amzel, L.M.
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	Description: Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound nitrite, obtained in the presence of substrate		Description: Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound nitrite, obtained in the presence of substrate

	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May ~~5 11~~:39:20 2010''		''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 12 10:45:51 2010''