4o29 - Revision history

OCA at 17:06, 20 September 2023

OCA — Wed, 20 Sep 2023 17:06:08 GMT

←Older revision		Revision as of 17:06, 20 September 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4o29]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrobaculum_aerophilum_str._IM2 Pyrobaculum aerophilum str. IM2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O29 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O29 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4o29]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrobaculum_aerophilum_str._IM2 Pyrobaculum aerophilum str. IM2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O29 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O29 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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]] 2.9Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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=4o29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o29 OCA], [https://pdbe.org/4o29 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o29 RCSB], [https://www.ebi.ac.uk/pdbsum/4o29 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o29 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=4o29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o29 OCA], [https://pdbe.org/4o29 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o29 RCSB], [https://www.ebi.ac.uk/pdbsum/4o29 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o29 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 08:53, 18 January 2023

OCA — Wed, 18 Jan 2023 08:53:07 GMT

←Older revision		Revision as of 08:53, 18 January 2023
Line 1:		Line 1:

	==PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE from Pyrobaculum aerophilum in COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE==		==PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE from Pyrobaculum aerophilum in COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE==
-	<StructureSection load='4o29' size='340' side='right' caption='[[4o29]], [[Resolution\|resolution]] 2.90Å' scene=''>	+	<StructureSection load='4o29' size='340' side='right'caption='[[4o29]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4o29]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Pyrae Pyrae~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O29 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4O29 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4o29]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrobaculum_aerophilum_str._IM2 Pyrobaculum aerophilum str. IM2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O29 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O29 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jg1\|1jg1]], [[2yxe\|2yxe]]</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=4o29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o29 OCA], [https://pdbe.org/4o29 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o29 RCSB], [https://www.ebi.ac.uk/pdbsum/4o29 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o29 ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PAE0701, pcm, PIMT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=178306 PYRAE])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-L-isoaspartate(D-aspartate)_O-methyltransferase Protein-L-isoaspartate(D-aspartate) O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.77 2.1.1.77] </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=4o29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o29 OCA], [~~http~~://pdbe.org/4o29 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4o29 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4o29 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4o29 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PIMT_PYRAE PIMT_PYRAE]] Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins (By similarity).	+	[https://www.uniprot.org/uniprot/PIMT_PYRAE PIMT_PYRAE] Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins (By similarity).
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Pyrae~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Griffith, S C~~]]	+	[[Category: Pyrobaculum aerophilum str. IM2]]
-	[[Category: ~~Sawaya, M R~~]]	+	[[Category: Griffith SC]]
-	[[Category: ~~Yeates, T O~~]]	+	[[Category: Sawaya MR]]
-	[[Category: ~~Protein repair isomerization]]~~	+	[[Category: Yeates TO]]
-	~~[[Category: Rossmann methyltransferase]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 16:23, 5 August 2016

OCA — Fri, 05 Aug 2016 16:23:05 GMT

←Older revision		Revision as of 16:23, 5 August 2016
Line 1:		Line 1:
		+
	==PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE from Pyrobaculum aerophilum in COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE==		==PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE from Pyrobaculum aerophilum in COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE==
	<StructureSection load='4o29' size='340' side='right' caption='[[4o29]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='4o29' size='340' side='right' caption='[[4o29]], [[Resolution\|resolution]] 2.90Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PAE0701, pcm, PIMT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=178306 PYRAE])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PAE0701, pcm, PIMT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=178306 PYRAE])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-L-isoaspartate(D-aspartate)_O-methyltransferase Protein-L-isoaspartate(D-aspartate) O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.77 2.1.1.77] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-L-isoaspartate(D-aspartate)_O-methyltransferase Protein-L-isoaspartate(D-aspartate) O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.77 2.1.1.77] </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=4o29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o29 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o29 RCSB], [http://www.ebi.ac.uk/pdbsum/4o29 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=4o29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o29 OCA], [http://pdbe.org/4o29 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o29 RCSB], [http://www.ebi.ac.uk/pdbsum/4o29 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o29 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 03:57, 25 December 2014

OCA — Thu, 25 Dec 2014 03:57:20 GMT

←Older revision		Revision as of 03:57, 25 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=4o29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o29 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o29 RCSB], [http://www.ebi.ac.uk/pdbsum/4o29 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=4o29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o29 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o29 RCSB], [http://www.ebi.ac.uk/pdbsum/4o29 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PIMT_PYRAE PIMT_PYRAE]] Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins (By similarity).
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 17:06, 21 December 2014

OCA — Sun, 21 Dec 2014 17:06:26 GMT

←Older revision		Revision as of 17:06, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4o29\| PDB=4o29 \| SCENE= }}~~	+	==PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE from Pyrobaculum aerophilum in COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE==
-	===PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE from Pyrobaculum aerophilum in COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE===	+	<StructureSection load='4o29' size='340' side='right' caption='[[4o29]], [[Resolution\|resolution]] 2.90Å' scene=''>
-		+	== Structural highlights ==
-	==~~Function~~==	+	<table><tr><td colspan='2'>[[4o29]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrae Pyrae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O29 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O29 FirstGlance]. <br>
-	[[http://~~www~~.~~uniprot~~.org/~~uniprot~~/~~PIMT_PYRAE PIMT_PYRAE~~]~~] Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result~~ from ~~spontaneous decomposition of normal L~~-~~aspartyl and L-asparaginyl residues~~. ~~It plays~~ a ~~role in~~ the ~~repair and~~/~~or degradation of damaged proteins (By similarity)~~.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
-		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jg1\|1jg1]], [[2yxe\|2yxe]]</td></tr>
-	==~~About this Structure~~==	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PAE0701, pcm, PIMT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=178306 PYRAE])</td></tr>
-	[[~~4o29~~]] ~~is a~~ 1 ~~chain structure~~. ~~Full crystallographic information is available from~~ [http://oca.weizmann.ac.il/oca-bin/~~ocashort~~?id=~~4O29~~ OCA].	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-L-isoaspartate(D-aspartate)_O-methyltransferase Protein-L-isoaspartate(D-aspartate) O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.77 2.1.1.77] </span></td></tr>
-	[[Category: Griffith, S C.]]	+	<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=4o29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o29 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o29 RCSB], [http://www.ebi.ac.uk/pdbsum/4o29 PDBsum]</span></td></tr>
-	[[Category: Sawaya, M R.]]	+	</table>
-	[[Category: Yeates, T O.]]	+	__TOC__
		+	</StructureSection>
		+	[[Category: Pyrae]]
		+	[[Category: Griffith, S C]]
		+	[[Category: Sawaya, M R]]
		+	[[Category: Yeates, T O]]
	[[Category: Protein repair isomerization]]		[[Category: Protein repair isomerization]]
	[[Category: Rossmann methyltransferase]]		[[Category: Rossmann methyltransferase]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 08:28, 15 January 2014

OCA — Wed, 15 Jan 2014 08:28:23 GMT

←Older revision		Revision as of 08:28, 15 January 2014
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4o29\| PDB=4o29 \| SCENE= }}
		+	===PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE from Pyrobaculum aerophilum in COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE===

-	~~The entry 4o29 is ON HOLD~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/PIMT_PYRAE PIMT_PYRAE]] Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins (By similarity).

-	~~Authors~~: Sawaya, ~~Michael~~ R., Yeates, ~~Todd~~ O.~~, Griffith, Scott C.~~	+	==About this Structure==
-		+	[[4o29]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O29 OCA].
-	~~Description~~: ~~PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE from Pyrobaculum aerophilum in COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE~~	+	[[Category: Griffith, S C.]]
		+	[[Category: Sawaya, M R.]]
		+	[[Category: Yeates, T O.]]
		+	[[Category: Protein repair isomerization]]
		+	[[Category: Rossmann methyltransferase]]
		+	[[Category: Transferase]]

OCA: Protected "4o29" [edit=sysop:move=sysop]

OCA — Wed, 25 Dec 2013 09:31:10 GMT

Protected "4o29" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:31, 25 December 2013

OCA: New page: '''Unreleased structure''' The entry 4o29 is ON HOLD Authors: Sawaya, Michael R., Yeates, Todd O., Griffith, Scott C. Description: PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE from Pyrob...

OCA — Wed, 25 Dec 2013 09:31:08 GMT

New page: '''Unreleased structure''' The entry 4o29 is ON HOLD Authors: Sawaya, Michael R., Yeates, Todd O., Griffith, Scott C. Description: PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE from Pyrob...

New page

'''Unreleased structure'''

The entry 4o29 is ON HOLD

Authors: Sawaya, Michael R., Yeates, Todd O., Griffith, Scott C.

Description: PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE from Pyrobaculum aerophilum in COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE