2bxr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:47, 23 October 2024) (edit) (undo)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
-
==HUMAN MONOAMINE OXIDASE A IN COMPLEX WITH CLORGYLINE, CRYSTAL FORM A==
+
 
-
<StructureSection load='2bxr' size='340' side='right' caption='[[2bxr]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+
==Human Monoamine Oxidase A in complex with Clorgyline, Crystal Form A==
 +
<StructureSection load='2bxr' size='340' side='right'caption='[[2bxr]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[2bxr]] 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=2BXR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BXR FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[2bxr]] 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=2BXR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BXR FirstGlance]. <br>
-
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MLG:N-[3-(2,4-DICHLOROPHENOXY)PROPYL]-N-METHYL-N-PROP-2-YNYLAMINE'>MLG</scene><br>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
-
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1h8q|1h8q]], [[2bxs|2bxs]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MLG:N-[3-(2,4-DICHLOROPHENOXY)PROPYL]-N-METHYL-N-PROP-2-YNYLAMINE'>MLG</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bxr OCA], [https://pdbe.org/2bxr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bxr RCSB], [https://www.ebi.ac.uk/pdbsum/2bxr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bxr ProSAT]</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=2bxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bxr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bxr RCSB], [http://www.ebi.ac.uk/pdbsum/2bxr PDBsum]</span></td></tr>
+
</table>
-
<table>
+
== Disease ==
== Disease ==
-
[[http://www.uniprot.org/uniprot/AOFA_HUMAN AOFA_HUMAN]] Defects in MAOA are the cause of Brunner syndrome (BRUNS) [MIM:[http://omim.org/entry/300615 300615]]. Brunner syndrome is a form of X-linked non-dysmorphic mild mental retardation. Male patients are affected by a syndrome of borderline mental retardation and exhibit abnormal behavior, including disturbed regulation of impulsive aggression. Obligate female carriers have normal intelligence and behavior.
+
[https://www.uniprot.org/uniprot/AOFA_HUMAN AOFA_HUMAN] Defects in MAOA are the cause of Brunner syndrome (BRUNS) [MIM:[https://omim.org/entry/300615 300615]. Brunner syndrome is a form of X-linked non-dysmorphic mild mental retardation. Male patients are affected by a syndrome of borderline mental retardation and exhibit abnormal behavior, including disturbed regulation of impulsive aggression. Obligate female carriers have normal intelligence and behavior.
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/AOFA_HUMAN AOFA_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. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine.
+
[https://www.uniprot.org/uniprot/AOFA_HUMAN AOFA_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. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
-
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bx/2bxr_consurf.spt"</scriptWhenChecked>
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bx/2bxr_consurf.spt"</scriptWhenChecked>
-
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
<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=2bxr ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
Line 30: Line 30:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
 +
<div class="pdbe-citations 2bxr" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
Line 38: Line 39:
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Monoamine oxidase]]
+
[[Category: Large Structures]]
-
[[Category: Binda, C.]]
+
[[Category: Binda C]]
-
[[Category: Colibus, L De.]]
+
[[Category: De Colibus L]]
-
[[Category: Edmondson, D E.]]
+
[[Category: Edmondson DE]]
-
[[Category: Mattevi, A.]]
+
[[Category: Mattevi A]]
-
[[Category: Flavin]]
+
-
[[Category: Membrane-protein]]
+
-
[[Category: Neurotransmitter]]
+
-
[[Category: Oxidoreductase]]
+

Current revision

Human Monoamine Oxidase A in complex with Clorgyline, Crystal Form A

PDB ID 2bxr

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bxr"
Personal tools