2xfo - Revision history

OCA at 10:30, 20 December 2023

OCA — Wed, 20 Dec 2023 10:30:35 GMT

←Older revision		Revision as of 10:30, 20 December 2023
Line 3:		Line 3:
	<StructureSection load='2xfo' size='340' side='right'caption='[[2xfo]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='2xfo' size='340' side='right'caption='[[2xfo]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2xfo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XFO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2xfo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XFO FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PL:3-PHENYLPROPANAL'>3PL</scene>, <scene name='pdbligand=FA8:[[(2R,3S,4S)-5-[(4AS)-7,8-DIMETHYL-2,4-DIOXO-4A,5-DIHYDROBENZO[G]PTERIDIN-10-YL]-2,3,4-TRIHYDROXY-PENTOXY]-HYDROXY-PHOSPHORYL]+[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL+HYDROGEN+PHOSPHATE'>FA8</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=XCG:2-(2-BENZOFURANYL)-2-IMIDAZOLINE'>XCG</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]] 2.1Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2c67\|2c67]], [[1oja\|1oja]], [[2v5z\|2v5z]], [[1s3e\|1s3e]], [[2c73\|2c73]], [[1ojb\|1ojb]], [[2v60\|2v60]], [[2byb\|2byb]], [[2vrm\|2vrm]], [[2c65\|2c65]], [[2c64\|2c64]], [[2xcg\|2xcg]], [[1oj9\|1oj9]], [[2vz2\|2vz2]], [[1ojd\|1ojd]], [[1s3b\|1s3b]], [[2c66\|2c66]], [[2bk4\|2bk4]], [[2bk5\|2bk5]], [[1h8r\|1h8r]], [[2c70\|2c70]], [[2bk3\|2bk3]], [[2c75\|2c75]], [[2v61\|2v61]], [[2c72\|2c72]], [[1s2y\|1s2y]], [[1gos\|1gos]], [[1s2q\|1s2q]], [[2c76\|2c76]], [[2vrl\|2vrl]], [[1ojc\|1ojc]], [[2xfq\|2xfq]], [[2xfn\|2xfn]], [[2xfp\|2xfp]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PL:3-PHENYLPROPANAL'>3PL</scene>, <scene name='pdbligand=FA8:[[(2R,3S,4S)-5-[(4AS)-7,8-DIMETHYL-2,4-DIOXO-4A,5-DIHYDROBENZO[G]PTERIDIN-10-YL]-2,3,4-TRIHYDROXY-PENTOXY]-HYDROXY-PHOSPHORYL]+[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL+HYDROGEN+PHOSPHATE'>FA8</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=XCG:2-(2-BENZOFURANYL)-2-IMIDAZOLINE'>XCG</scene></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MAOB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </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=2xfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xfo OCA], [https://pdbe.org/2xfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xfo RCSB], [https://www.ebi.ac.uk/pdbsum/2xfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xfo 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=2xfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xfo OCA], [https://pdbe.org/2xfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xfo RCSB], [https://www.ebi.ac.uk/pdbsum/2xfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xfo ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/AOFB_HUMAN AOFB_HUMAN]] Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine.	+	[https://www.uniprot.org/uniprot/AOFB_HUMAN AOFB_HUMAN] Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Monoamine oxidase]]~~	+	[[Category: Binda C]]
-	[[Category: Binda, C]]	+	[[Category: Bonivento D]]
-	[[Category: Bonivento, D]]	+	[[Category: Edmondson DE]]
-	[[Category: Edmondson~~, D E~~]]	+	[[Category: Holt A]]
-	[[Category: Holt, A]]	+	[[Category: Mattevi A]]
-	[[Category: Mattevi, A]]	+	[[Category: McDonald GR]]
-	[[Category: McDonald~~, G R~~]]	+	[[Category: Milczek EM]]
-	[[Category: Milczek~~, E M]]~~	+
-	~~[[Category: Flavoprotein]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 08:39, 10 November 2021

OCA — Wed, 10 Nov 2021 08:39:40 GMT

←Older revision		Revision as of 08:39, 10 November 2021
Line 1:		Line 1:

	==tranylcypromine-inhibited human monoamine oxidase B Ile199Ala mutant in complex with 2-(2-benzofuranyl)-2-imidazoline==		==tranylcypromine-inhibited human monoamine oxidase B Ile199Ala mutant in complex with 2-(2-benzofuranyl)-2-imidazoline==
-	<StructureSection load='2xfo' size='340' side='right' caption='[[2xfo]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='2xfo' size='340' side='right'caption='[[2xfo]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2xfo]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XFO OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2XFO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2xfo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XFO FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3PL:3-PHENYLPROPANAL'>3PL</scene>, <scene name='pdbligand=FA8:[[(2R,3S,4S)-5-[(4AS)-7,8-DIMETHYL-2,4-DIOXO-4A,5-DIHYDROBENZO[G]PTERIDIN-10-YL]-2,3,4-TRIHYDROXY-PENTOXY]-HYDROXY-PHOSPHORYL]+[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL+HYDROGEN+PHOSPHATE'>FA8</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=XCG:2-(2-BENZOFURANYL)-2-IMIDAZOLINE'>XCG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PL:3-PHENYLPROPANAL'>3PL</scene>, <scene name='pdbligand=FA8:[[(2R,3S,4S)-5-[(4AS)-7,8-DIMETHYL-2,4-DIOXO-4A,5-DIHYDROBENZO[G]PTERIDIN-10-YL]-2,3,4-TRIHYDROXY-PENTOXY]-HYDROXY-PHOSPHORYL]+[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL+HYDROGEN+PHOSPHATE'>FA8</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=XCG:2-(2-BENZOFURANYL)-2-IMIDAZOLINE'>XCG</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2c67\|2c67]], [[1oja\|1oja]], [[2v5z\|2v5z]], [[1s3e\|1s3e]], [[2c73\|2c73]], [[1ojb\|1ojb]], [[2v60\|2v60]], [[2byb\|2byb]], [[2vrm\|2vrm]], [[2c65\|2c65]], [[2c64\|2c64]], [[2xcg\|2xcg]], [[1oj9\|1oj9]], [[2vz2\|2vz2]], [[1ojd\|1ojd]], [[1s3b\|1s3b]], [[2c66\|2c66]], [[2bk4\|2bk4]], [[2bk5\|2bk5]], [[1h8r\|1h8r]], [[2c70\|2c70]], [[2bk3\|2bk3]], [[2c75\|2c75]], [[2v61\|2v61]], [[2c72\|2c72]], [[1s2y\|1s2y]], [[1gos\|1gos]], [[1s2q\|1s2q]], [[2c76\|2c76]], [[2vrl\|2vrl]], [[1ojc\|1ojc]], [[2xfq\|2xfq]], [[2xfn\|2xfn]], [[2xfp\|2xfp]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2c67\|2c67]], [[1oja\|1oja]], [[2v5z\|2v5z]], [[1s3e\|1s3e]], [[2c73\|2c73]], [[1ojb\|1ojb]], [[2v60\|2v60]], [[2byb\|2byb]], [[2vrm\|2vrm]], [[2c65\|2c65]], [[2c64\|2c64]], [[2xcg\|2xcg]], [[1oj9\|1oj9]], [[2vz2\|2vz2]], [[1ojd\|1ojd]], [[1s3b\|1s3b]], [[2c66\|2c66]], [[2bk4\|2bk4]], [[2bk5\|2bk5]], [[1h8r\|1h8r]], [[2c70\|2c70]], [[2bk3\|2bk3]], [[2c75\|2c75]], [[2v61\|2v61]], [[2c72\|2c72]], [[1s2y\|1s2y]], [[1gos\|1gos]], [[1s2q\|1s2q]], [[2c76\|2c76]], [[2vrl\|2vrl]], [[1ojc\|1ojc]], [[2xfq\|2xfq]], [[2xfn\|2xfn]], [[2xfp\|2xfp]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MAOB ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MAOB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </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=2xfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xfo OCA], [~~http~~://pdbe.org/2xfo PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2xfo RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2xfo PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2xfo 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=2xfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xfo OCA], [https://pdbe.org/2xfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xfo RCSB], [https://www.ebi.ac.uk/pdbsum/2xfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xfo ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/AOFB_HUMAN AOFB_HUMAN]] Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine.	+	[[https://www.uniprot.org/uniprot/AOFB_HUMAN AOFB_HUMAN]] Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Monoamine oxidase]]		[[Category: Monoamine oxidase]]
	[[Category: Binda, C]]		[[Category: Binda, C]]

OCA at 07:25, 25 July 2018

OCA — Wed, 25 Jul 2018 07:25:53 GMT

←Older revision		Revision as of 07:25, 25 July 2018
Line 3:		Line 3:
	<StructureSection load='2xfo' size='340' side='right' caption='[[2xfo]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='2xfo' size='340' side='right' caption='[[2xfo]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2xfo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XFO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XFO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2xfo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XFO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XFO FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3PL:3-PHENYLPROPANAL'>3PL</scene>, <scene name='pdbligand=FA8:[[(2R,3S,4S)-5-[(4AS)-7,8-DIMETHYL-2,4-DIOXO-4A,5-DIHYDROBENZO[G]PTERIDIN-10-YL]-2,3,4-TRIHYDROXY-PENTOXY]-HYDROXY-PHOSPHORYL]+[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL+HYDROGEN+PHOSPHATE'>FA8</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=XCG:2-(2-BENZOFURANYL)-2-IMIDAZOLINE'>XCG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3PL:3-PHENYLPROPANAL'>3PL</scene>, <scene name='pdbligand=FA8:[[(2R,3S,4S)-5-[(4AS)-7,8-DIMETHYL-2,4-DIOXO-4A,5-DIHYDROBENZO[G]PTERIDIN-10-YL]-2,3,4-TRIHYDROXY-PENTOXY]-HYDROXY-PHOSPHORYL]+[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL+HYDROGEN+PHOSPHATE'>FA8</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=XCG:2-(2-BENZOFURANYL)-2-IMIDAZOLINE'>XCG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2c67\|2c67]], [[1oja\|1oja]], [[2v5z\|2v5z]], [[1s3e\|1s3e]], [[2c73\|2c73]], [[1ojb\|1ojb]], [[2v60\|2v60]], [[2byb\|2byb]], [[2vrm\|2vrm]], [[2c65\|2c65]], [[2c64\|2c64]], [[2xcg\|2xcg]], [[1oj9\|1oj9]], [[2vz2\|2vz2]], [[1ojd\|1ojd]], [[1s3b\|1s3b]], [[2c66\|2c66]], [[2bk4\|2bk4]], [[2bk5\|2bk5]], [[1h8r\|1h8r]], [[2c70\|2c70]], [[2bk3\|2bk3]], [[2c75\|2c75]], [[2v61\|2v61]], [[2c72\|2c72]], [[1s2y\|1s2y]], [[1gos\|1gos]], [[1s2q\|1s2q]], [[2c76\|2c76]], [[2vrl\|2vrl]], [[1ojc\|1ojc]], [[2xfq\|2xfq]], [[2xfn\|2xfn]], [[2xfp\|2xfp]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2c67\|2c67]], [[1oja\|1oja]], [[2v5z\|2v5z]], [[1s3e\|1s3e]], [[2c73\|2c73]], [[1ojb\|1ojb]], [[2v60\|2v60]], [[2byb\|2byb]], [[2vrm\|2vrm]], [[2c65\|2c65]], [[2c64\|2c64]], [[2xcg\|2xcg]], [[1oj9\|1oj9]], [[2vz2\|2vz2]], [[1ojd\|1ojd]], [[1s3b\|1s3b]], [[2c66\|2c66]], [[2bk4\|2bk4]], [[2bk5\|2bk5]], [[1h8r\|1h8r]], [[2c70\|2c70]], [[2bk3\|2bk3]], [[2c75\|2c75]], [[2v61\|2v61]], [[2c72\|2c72]], [[1s2y\|1s2y]], [[1gos\|1gos]], [[1s2q\|1s2q]], [[2c76\|2c76]], [[2vrl\|2vrl]], [[1ojc\|1ojc]], [[2xfq\|2xfq]], [[2xfn\|2xfn]], [[2xfp\|2xfp]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MAOB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </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=2xfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xfo OCA], [http://pdbe.org/2xfo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xfo RCSB], [http://www.ebi.ac.uk/pdbsum/2xfo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xfo ProSAT]</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=2xfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xfo OCA], [http://pdbe.org/2xfo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xfo RCSB], [http://www.ebi.ac.uk/pdbsum/2xfo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xfo ProSAT]</span></td></tr>
Line 37:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Monoamine oxidase]]		[[Category: Monoamine oxidase]]
	[[Category: Binda, C]]		[[Category: Binda, C]]

OCA at 05:39, 16 May 2018

OCA — Wed, 16 May 2018 05:39:55 GMT

←Older revision		Revision as of 05:39, 16 May 2018
Line 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 2xfo" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2xfo" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Monoamine oxidase\|Monoamine oxidase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:33, 20 December 2017

OCA — Wed, 20 Dec 2017 06:33:10 GMT

←Older revision		Revision as of 06:33, 20 December 2017
Line 1:		Line 1:

-	==~~TRANYLCYPROMINE~~-~~INHIBITED HUMAN MONOAMINE OXIDASE~~ B ~~ILE199ALA MUTANT IN COMPLEX WITH~~ 2-(2-~~BENZOFURANYL~~)-2-~~IMIDAZOLINE~~==	+	==tranylcypromine-inhibited human monoamine oxidase B Ile199Ala mutant in complex with 2-(2-benzofuranyl)-2-imidazoline==
	<StructureSection load='2xfo' size='340' side='right' caption='[[2xfo]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='2xfo' size='340' side='right' caption='[[2xfo]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xf/2xfo_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xf/2xfo_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 2xfo" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2xfo" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Monoamine oxidase\|Monoamine oxidase]]
	== References ==		== References ==
	<references/>		<references/>
Line 44:		Line 41:
	[[Category: Holt, A]]		[[Category: Holt, A]]
	[[Category: Mattevi, A]]		[[Category: Mattevi, A]]
-	[[Category: ~~Mcdonald~~, G R]]	+	[[Category: McDonald, G R]]
	[[Category: Milczek, E M]]		[[Category: Milczek, E M]]
	[[Category: Flavoprotein]]		[[Category: Flavoprotein]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 13:34, 4 August 2016

OCA — Thu, 04 Aug 2016 13:34:03 GMT

←Older revision		Revision as of 13:34, 4 August 2016
Line 1:		Line 1:
		+
	==TRANYLCYPROMINE-INHIBITED HUMAN MONOAMINE OXIDASE B ILE199ALA MUTANT IN COMPLEX WITH 2-(2-BENZOFURANYL)-2-IMIDAZOLINE==		==TRANYLCYPROMINE-INHIBITED HUMAN MONOAMINE OXIDASE B ILE199ALA MUTANT IN COMPLEX WITH 2-(2-BENZOFURANYL)-2-IMIDAZOLINE==
	<StructureSection load='2xfo' size='340' side='right' caption='[[2xfo]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='2xfo' size='340' side='right' caption='[[2xfo]], [[Resolution\|resolution]] 2.10Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2c67\|2c67]], [[1oja\|1oja]], [[2v5z\|2v5z]], [[1s3e\|1s3e]], [[2c73\|2c73]], [[1ojb\|1ojb]], [[2v60\|2v60]], [[2byb\|2byb]], [[2vrm\|2vrm]], [[2c65\|2c65]], [[2c64\|2c64]], [[2xcg\|2xcg]], [[1oj9\|1oj9]], [[2vz2\|2vz2]], [[1ojd\|1ojd]], [[1s3b\|1s3b]], [[2c66\|2c66]], [[2bk4\|2bk4]], [[2bk5\|2bk5]], [[1h8r\|1h8r]], [[2c70\|2c70]], [[2bk3\|2bk3]], [[2c75\|2c75]], [[2v61\|2v61]], [[2c72\|2c72]], [[1s2y\|1s2y]], [[1gos\|1gos]], [[1s2q\|1s2q]], [[2c76\|2c76]], [[2vrl\|2vrl]], [[1ojc\|1ojc]], [[2xfq\|2xfq]], [[2xfn\|2xfn]], [[2xfp\|2xfp]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2c67\|2c67]], [[1oja\|1oja]], [[2v5z\|2v5z]], [[1s3e\|1s3e]], [[2c73\|2c73]], [[1ojb\|1ojb]], [[2v60\|2v60]], [[2byb\|2byb]], [[2vrm\|2vrm]], [[2c65\|2c65]], [[2c64\|2c64]], [[2xcg\|2xcg]], [[1oj9\|1oj9]], [[2vz2\|2vz2]], [[1ojd\|1ojd]], [[1s3b\|1s3b]], [[2c66\|2c66]], [[2bk4\|2bk4]], [[2bk5\|2bk5]], [[1h8r\|1h8r]], [[2c70\|2c70]], [[2bk3\|2bk3]], [[2c75\|2c75]], [[2v61\|2v61]], [[2c72\|2c72]], [[1s2y\|1s2y]], [[1gos\|1gos]], [[1s2q\|1s2q]], [[2c76\|2c76]], [[2vrl\|2vrl]], [[1ojc\|1ojc]], [[2xfq\|2xfq]], [[2xfn\|2xfn]], [[2xfp\|2xfp]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </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=2xfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xfo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xfo RCSB], [http://www.ebi.ac.uk/pdbsum/2xfo 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=2xfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xfo OCA], [http://pdbe.org/2xfo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xfo RCSB], [http://www.ebi.ac.uk/pdbsum/2xfo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xfo ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2xfo ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 28:		Line 29:
	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 2xfo" style="background-color:#fffaf0;"></div>

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

OCA at 15:06, 24 December 2014

OCA — Wed, 24 Dec 2014 15:06:04 GMT

←Older revision		Revision as of 15:06, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2xfo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XFO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XFO FirstGlance]. <br>		<table><tr><td colspan='2'>[[2xfo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XFO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XFO FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3PL:3-PHENYLPROPANAL'>3PL</scene>, <scene name='pdbligand=FA8:[[(2R,3S,4S)-5-[(4AS)-7,8-DIMETHYL-2,4-DIOXO-4A,5-DIHYDROBENZO[G]PTERIDIN-10-YL]-2,3,4-TRIHYDROXY-PENTOXY]-HYDROXY-PHOSPHORYL]+[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL+HYDROGEN+PHOSPHATE'>FA8</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=XCG:2-(2-BENZOFURANYL)-2-IMIDAZOLINE'>XCG</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3PL:3-PHENYLPROPANAL'>3PL</scene>, <scene name='pdbligand=FA8:[[(2R,3S,4S)-5-[(4AS)-7,8-DIMETHYL-2,4-DIOXO-4A,5-DIHYDROBENZO[G]PTERIDIN-10-YL]-2,3,4-TRIHYDROXY-PENTOXY]-HYDROXY-PHOSPHORYL]+[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL+HYDROGEN+PHOSPHATE'>FA8</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=XCG:2-(2-BENZOFURANYL)-2-IMIDAZOLINE'>XCG</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2c67\|2c67]], [[1oja\|1oja]], [[2v5z\|2v5z]], [[1s3e\|1s3e]], [[2c73\|2c73]], [[1ojb\|1ojb]], [[2v60\|2v60]], [[2byb\|2byb]], [[2vrm\|2vrm]], [[2c65\|2c65]], [[2c64\|2c64]], [[2xcg\|2xcg]], [[1oj9\|1oj9]], [[2vz2\|2vz2]], [[1ojd\|1ojd]], [[1s3b\|1s3b]], [[2c66\|2c66]], [[2bk4\|2bk4]], [[2bk5\|2bk5]], [[1h8r\|1h8r]], [[2c70\|2c70]], [[2bk3\|2bk3]], [[2c75\|2c75]], [[2v61\|2v61]], [[2c72\|2c72]], [[1s2y\|1s2y]], [[1gos\|1gos]], [[1s2q\|1s2q]], [[2c76\|2c76]], [[2vrl\|2vrl]], [[1ojc\|1ojc]], [[2xfq\|2xfq]], [[2xfn\|2xfn]], [[2xfp\|2xfp]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2c67\|2c67]], [[1oja\|1oja]], [[2v5z\|2v5z]], [[1s3e\|1s3e]], [[2c73\|2c73]], [[1ojb\|1ojb]], [[2v60\|2v60]], [[2byb\|2byb]], [[2vrm\|2vrm]], [[2c65\|2c65]], [[2c64\|2c64]], [[2xcg\|2xcg]], [[1oj9\|1oj9]], [[2vz2\|2vz2]], [[1ojd\|1ojd]], [[1s3b\|1s3b]], [[2c66\|2c66]], [[2bk4\|2bk4]], [[2bk5\|2bk5]], [[1h8r\|1h8r]], [[2c70\|2c70]], [[2bk3\|2bk3]], [[2c75\|2c75]], [[2v61\|2v61]], [[2c72\|2c72]], [[1s2y\|1s2y]], [[1gos\|1gos]], [[1s2q\|1s2q]], [[2c76\|2c76]], [[2vrl\|2vrl]], [[1ojc\|1ojc]], [[2xfq\|2xfq]], [[2xfn\|2xfn]], [[2xfp\|2xfp]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xfo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xfo RCSB], [http://www.ebi.ac.uk/pdbsum/2xfo 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=2xfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xfo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xfo RCSB], [http://www.ebi.ac.uk/pdbsum/2xfo PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/AOFB_HUMAN AOFB_HUMAN]] Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 37:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Monoamine oxidase]]		[[Category: Monoamine oxidase]]
-	[[Category: Binda, C.]]	+	[[Category: Binda, C]]
-	[[Category: Bonivento, D.]]	+	[[Category: Bonivento, D]]
-	[[Category: Edmondson, D E.]]	+	[[Category: Edmondson, D E]]
-	[[Category: Holt, A.]]	+	[[Category: Holt, A]]
-	[[Category: Mattevi, A.]]	+	[[Category: Mattevi, A]]
-	[[Category: Mcdonald, G R.]]	+	[[Category: Mcdonald, G R]]
-	[[Category: Milczek, E M.]]	+	[[Category: Milczek, E M]]
	[[Category: Flavoprotein]]		[[Category: Flavoprotein]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 00:57, 2 October 2014

OCA — Thu, 02 Oct 2014 00:57:27 GMT

←Older revision		Revision as of 00:57, 2 October 2014
Line 1:		Line 1:
-	[[~~Image:~~2xfo.~~png~~\|~~left~~\|200px]]	+	==TRANYLCYPROMINE-INHIBITED HUMAN MONOAMINE OXIDASE B ILE199ALA MUTANT IN COMPLEX WITH 2-(2-BENZOFURANYL)-2-IMIDAZOLINE==
		+	<StructureSection load='2xfo' size='340' side='right' caption='[[2xfo]], [[Resolution\|resolution]] 2.10Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2xfo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XFO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XFO FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3PL:3-PHENYLPROPANAL'>3PL</scene>, <scene name='pdbligand=FA8:[[(2R,3S,4S)-5-[(4AS)-7,8-DIMETHYL-2,4-DIOXO-4A,5-DIHYDROBENZO[G]PTERIDIN-10-YL]-2,3,4-TRIHYDROXY-PENTOXY]-HYDROXY-PHOSPHORYL]+[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL+HYDROGEN+PHOSPHATE'>FA8</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=XCG:2-(2-BENZOFURANYL)-2-IMIDAZOLINE'>XCG</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2c67\|2c67]], [[1oja\|1oja]], [[2v5z\|2v5z]], [[1s3e\|1s3e]], [[2c73\|2c73]], [[1ojb\|1ojb]], [[2v60\|2v60]], [[2byb\|2byb]], [[2vrm\|2vrm]], [[2c65\|2c65]], [[2c64\|2c64]], [[2xcg\|2xcg]], [[1oj9\|1oj9]], [[2vz2\|2vz2]], [[1ojd\|1ojd]], [[1s3b\|1s3b]], [[2c66\|2c66]], [[2bk4\|2bk4]], [[2bk5\|2bk5]], [[1h8r\|1h8r]], [[2c70\|2c70]], [[2bk3\|2bk3]], [[2c75\|2c75]], [[2v61\|2v61]], [[2c72\|2c72]], [[1s2y\|1s2y]], [[1gos\|1gos]], [[1s2q\|1s2q]], [[2c76\|2c76]], [[2vrl\|2vrl]], [[1ojc\|1ojc]], [[2xfq\|2xfq]], [[2xfn\|2xfn]], [[2xfp\|2xfp]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xfo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xfo RCSB], [http://www.ebi.ac.uk/pdbsum/2xfo PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xf/2xfo_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Crystallographic and biochemical studies have been employed to identify the binding site and mechanism for potentiation of imidazoline-binding in human monoamine oxidase B (MAO B). 2-(2-Benzofuranyl)-2-imidazoline (2-BFI) inhibits recombinant human MAO B with a Ki of 8.3+/-0.6 muM whereas tranylcypromine-inhibited MAO B binds 2-BFI with a Kd of 9+/-2 nM, representing an increase in binding energy Delta(DeltaG) of -3.9 kcal/mol. Crystal structures show the imidazoline ligand bound in a site that is distinct from the substrate-binding cavity. Contributions to account for the increase in binding affinity upon tranylcypromine inhibition include a conformational change in the side chain of Gln206 and a "closed conformation" of the side chain of Ile199, forming a hydrophobic "sandwich" with the side chain of Ile316 on each face of the benzofuran ring of 2-BFI. Data with the Ile199Ala mutant of human MAO B and failure to observe a similar binding potentiation with rat MAO B, where Ile316 is replaced with a Val residue, support an allosteric mechanism where the increased binding affinity of 2-BFI results from a cooperative increase in H-bond strength through formation of a more hydrophobic milieu. These insights should prove valuable in the design of high affinity and specific reversible MAO B inhibitors.

-	~~{{STRUCTURE_2xfo\| PDB=2xfo \| SCENE= }}~~	+	Potentiation of ligand binding through cooperative effects in monoamine oxidase B.,Bonivento D, Milczek EM, McDonald GR, Binda C, Holt A, Edmondson DE, Mattevi A J Biol Chem. 2010 Sep 20. PMID:20855894<ref>PMID:20855894</ref>

-	~~===TRANYLCYPROMINE-INHIBITED HUMAN MONOAMINE OXIDASE B ILE199ALA MUTANT IN COMPLEX WITH 2-(2-BENZOFURANYL)-2-IMIDAZOLINE===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_20855894}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[2xfo]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2XFO OCA].~~	+

	==See Also==		==See Also==
	*[[Monoamine oxidase\|Monoamine oxidase]]		*[[Monoamine oxidase\|Monoamine oxidase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:020855894<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Monoamine oxidase]]		[[Category: Monoamine oxidase]]

OCA at 06:38, 20 October 2012

OCA — Sat, 20 Oct 2012 06:38:47 GMT

←Older revision		Revision as of 06:38, 20 October 2012
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	==About this Structure==		==About this Structure==
-	[[2xfo]] is a 2 chain structure ~~of [[Monoamine oxidase]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XFO OCA].	+	[[2xfo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XFO OCA].

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

OCA: Protected "2xfo" [edit=sysop:move=sysop]

OCA — Wed, 25 Jul 2012 13:52:22 GMT

Protected "2xfo" [edit=sysop:move=sysop]

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Revision as of 13:52, 25 July 2012