3mlj - Revision history

OCA at 08:55, 6 September 2023

OCA — Wed, 06 Sep 2023 08:55:38 GMT

←Older revision		Revision as of 08:55, 6 September 2023
Line 3:		Line 3:
	<StructureSection load='3mlj' size='340' side='right'caption='[[3mlj]], [[Resolution\|resolution]] 2.15Å' scene=''>		<StructureSection load='3mlj' size='340' side='right'caption='[[3mlj]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3mlj]] 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=3MLJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MLJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3mlj]] 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=3MLJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MLJ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <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~~></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]] 2.15Å</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]], [[3mig\|3mig]], [[3mih\|3mih]], [[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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <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></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=3mlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mlj OCA], [https://pdbe.org/3mlj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mlj RCSB], [https://www.ebi.ac.uk/pdbsum/3mlj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mlj 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=3mlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mlj OCA], [https://pdbe.org/3mlj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mlj RCSB], [https://www.ebi.ac.uk/pdbsum/3mlj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mlj 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 ==
Line 31:		Line 29:
	__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: Prigge~~, S T]]~~	+	[[Category: Prigge ST]]
-	~~[[Category: Ascorbate]]~~	+
-	~~[[Category: Bioactive peptide activation]]~~	+
-	~~[[Category: Monooxygenase]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 13:48, 4 May 2022

OCA — Wed, 04 May 2022 13:48:03 GMT

←Older revision		Revision as of 13:48, 4 May 2022
Line 1:		Line 1:

	==Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound carbon monooxide (CO)==		==Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound carbon monooxide (CO)==
-	<StructureSection load='3mlj' size='340' side='right' caption='[[3mlj]], [[Resolution\|resolution]] 2.15Å' scene=''>	+	<StructureSection load='3mlj' size='340' side='right'caption='[[3mlj]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3mlj]] 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=3MLJ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3MLJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3mlj]] 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=3MLJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MLJ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <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></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <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></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]], [[3mig\|3mig]], [[3mih\|3mih]], [[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]], [[3mig\|3mig]], [[3mih\|3mih]], [[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=3mlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mlj OCA], [~~http~~://pdbe.org/3mlj PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3mlj RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3mlj PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3mlj 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=3mlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mlj OCA], [https://pdbe.org/3mlj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mlj RCSB], [https://www.ebi.ac.uk/pdbsum/3mlj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mlj 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 ==
Line 24:		Line 24:
	==See Also==		==See Also==
	*[[Antibody 3D structures\|Antibody 3D structures]]		*[[Antibody 3D structures\|Antibody 3D structures]]
-	*[[Monooxygenase\|Monooxygenase]]	+	*[[Monooxygenase 3D structures\|Monooxygenase 3D structures]]
		+	*[[Sandbox 20009\|Sandbox 20009]]
		+	*[[3D structures of human antibody\|3D structures of human antibody]]
	== References ==		== References ==
	<references/>		<references/>
Line 30:		Line 32:
	</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 13:02, 16 January 2019

OCA — Wed, 16 Jan 2019 13:02:41 GMT

←Older revision		Revision as of 13:02, 16 January 2019
Line 23:		Line 23:

	==See Also==		==See Also==
-	*[[3D structures ~~of antibody~~\|3D structures ~~of antibody~~]]	+	*[[Antibody 3D structures\|Antibody 3D structures]]
		+	*[[Monooxygenase\|Monooxygenase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:46, 5 August 2016

OCA — Fri, 05 Aug 2016 06:46:53 GMT

←Older revision		Revision as of 06:46, 5 August 2016
Line 1:		Line 1:
		+
	==Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound carbon monooxide (CO)==		==Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound carbon monooxide (CO)==
	<StructureSection load='3mlj' size='340' side='right' caption='[[3mlj]], [[Resolution\|resolution]] 2.15Å' scene=''>		<StructureSection load='3mlj' size='340' side='right' caption='[[3mlj]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3mlj]] 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=3MLJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MLJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3mlj]] 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=3MLJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MLJ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <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></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <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></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]], [[3mig\|3mig]], [[3mih\|3mih]], [[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]], [[3mig\|3mig]], [[3mih\|3mih]], [[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=3mlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mlj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mlj RCSB], [http://www.ebi.ac.uk/pdbsum/3mlj 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=3mlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mlj OCA], [http://pdbe.org/3mlj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mlj RCSB], [http://www.ebi.ac.uk/pdbsum/3mlj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mlj 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 3mlj" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
-	*[[~~Antibody~~\|~~Antibody~~]]	+	*[[3D structures of antibody\|3D structures of antibody]]
	== 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 23:57, 24 December 2014

OCA — Wed, 24 Dec 2014 23:57:50 GMT

←Older revision		Revision as of 23:57, 24 December 2014
Line 9:		Line 9:
	<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=3mlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mlj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mlj RCSB], [http://www.ebi.ac.uk/pdbsum/3mlj 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=3mlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mlj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mlj RCSB], [http://www.ebi.ac.uk/pdbsum/3mlj 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 17:27, 18 December 2014

OCA — Thu, 18 Dec 2014 17:27:10 GMT

←Older revision		Revision as of 17:27, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3mlj\| PDB=3mlj \| SCENE= }}~~	+	==Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound carbon monooxide (CO)==
-	===Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound carbon monooxide (CO)===	+	<StructureSection load='3mlj' size='340' side='right' caption='[[3mlj]], [[Resolution\|resolution]] 2.15Å' scene=''>
-	~~{{ABSTRACT_PUBMED_20958070}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3mlj]] 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=3MLJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MLJ FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <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></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]], [[3mig\|3mig]], [[3mih\|3mih]], [[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=3mlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mlj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mlj RCSB], [http://www.ebi.ac.uk/pdbsum/3mlj 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>
-	~~[[3mlj]] 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=3MLJ OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:020958070</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[Antibody\|Antibody]]
		+	== References ==
		+	<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: Prigge, S T.]]	+	[[Category: Prigge, S T]]
	[[Category: Ascorbate]]		[[Category: Ascorbate]]
	[[Category: Bioactive peptide activation]]		[[Category: Bioactive peptide activation]]
	[[Category: Monooxygenase]]		[[Category: Monooxygenase]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 20:53, 17 April 2013

OCA — Wed, 17 Apr 2013 20:53:02 GMT

←Older revision		Revision as of 20:53, 17 April 2013
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-	[[Image:3mlj.jpg\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3mlj", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3mlj\| PDB=3mlj \| SCENE= }}		{{STRUCTURE_3mlj\| PDB=3mlj \| SCENE= }}
-
	===Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound carbon monooxide (CO)===		===Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound carbon monooxide (CO)===
		+	{{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==
Line 22:		Line 10:

	==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]]
Line 30:		Line 18:
	[[Category: Mains, R E.]]		[[Category: Mains, R E.]]
	[[Category: Prigge, S T.]]		[[Category: Prigge, S T.]]
		+	[[Category: Ascorbate]]
		+	[[Category: Bioactive peptide activation]]
		+	[[Category: Monooxygenase]]
		+	[[Category: Oxidoreductase]]

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

OCA — Wed, 02 Mar 2011 06:56:10 GMT

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

←Older revision

Revision as of 06:56, 2 March 2011

OCA at 06:56, 2 March 2011

OCA — Wed, 02 Mar 2011 06:56:06 GMT

←Older revision		Revision as of 06:56, 2 March 2011
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-	~~'''Unreleased structure'''~~	+	[[Image:3mlj.jpg\|left\|200px]]

-	The ~~entry 3mlj~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3mlj", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3mlj\| PDB=3mlj \| SCENE= }}

-	~~Authors: Prigge, S.T., Chufan, E.E., Eipper, B.A., Mains, R.E., Amzel, L.M.~~	+	===Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound carbon monooxide (CO)===

-	Description: Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound carbon monooxide (CO)

-	~~''Page seeded by~~ [http://oca.weizmann.ac.il/oca OCA ] ~~on Wed Aug 4 08~~:45:~~51 2010''~~	+	<!--
		+	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==
		+	[[3mlj]] 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=3MLJ OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:20958070</ref><references group="xtra"/>
		+	[[Category: Peptidylglycine monooxygenase]]
		+	[[Category: Rattus norvegicus]]
		+	[[Category: Amzel, L M.]]
		+	[[Category: Chufan, E E.]]
		+	[[Category: Eipper, B A.]]
		+	[[Category: Mains, R E.]]
		+	[[Category: Prigge, S T.]]

OCA at 04:38, 4 August 2010

OCA — Wed, 04 Aug 2010 04:38:52 GMT

←Older revision		Revision as of 04:38, 4 August 2010
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3mlj is ON HOLD	+	The entry 3mlj is ON HOLD until Paper Publication

	Authors: Prigge, S.T., Chufan, E.E., Eipper, B.A., Mains, R.E., Amzel, L.M.		Authors: Prigge, S.T., Chufan, E.E., Eipper, B.A., Mains, R.E., Amzel, L.M.
Line 7:		Line 7:
	Description: Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound carbon monooxide (CO)		Description: Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound carbon monooxide (CO)

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~May~~ ~~5 11~~:40:11 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 4 08:45:51 2010''