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2xlu

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==JOINT-FUNCTIONS OF PROTEIN RESIDUES AND NADP(H) IN OXYGEN-ACTIVATION BY FLAVIN-CONTAINING MONOOXYGENASE: COMPLEX WITH THIONADP==
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==Joint-functions of protein residues and NADP(H) in oxygen-activation by flavin-containing monooxygenase: complex with thioNADP==
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<StructureSection load='2xlu' size='340' side='right' caption='[[2xlu]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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<StructureSection load='2xlu' size='340' side='right'caption='[[2xlu]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2xlu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Jcm_14647 Jcm 14647]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XLU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XLU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2xlu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylophaga_aminisulfidivorans Methylophaga aminisulfidivorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XLU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XLU FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NA7:[(2R,3R,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-3-HYDROXY-4-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]METHYL+[(2R,3S,4S)-3,4-DIHYDROXYTETRAHYDROFURAN-2-YL]METHYL+DIHYDROGEN+DIPHOSPHATE'>NA7</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xlr|2xlr]], [[2vqb|2vqb]], [[2xlp|2xlp]], [[2vq7|2vq7]], [[2xlt|2xlt]], [[2xls|2xls]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NA7:[(2R,3R,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-3-HYDROXY-4-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]METHYL+[(2R,3S,4S)-3,4-DIHYDROXYTETRAHYDROFURAN-2-YL]METHYL+DIHYDROGEN+DIPHOSPHATE'>NA7</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Flavin-containing_monooxygenase Flavin-containing monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.8 1.14.13.8] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xlu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xlu OCA], [https://pdbe.org/2xlu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xlu RCSB], [https://www.ebi.ac.uk/pdbsum/2xlu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xlu ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xlu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xlu OCA], [http://pdbe.org/2xlu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xlu RCSB], [http://www.ebi.ac.uk/pdbsum/2xlu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xlu ProSAT]</span></td></tr>
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</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q83XK4_9GAMM Q83XK4_9GAMM]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xl/2xlu_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xl/2xlu_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>
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</div>
</div>
<div class="pdbe-citations 2xlu" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 2xlu" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Flavin-containing monooxygenase]]
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[[Category: Large Structures]]
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[[Category: Jcm 14647]]
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[[Category: Methylophaga aminisulfidivorans]]
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[[Category: Fraaije, M W]]
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[[Category: Fraaije MW]]
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[[Category: Mattevi, A]]
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[[Category: Mattevi A]]
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[[Category: Orru, R]]
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[[Category: Orru R]]
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[[Category: Oxidoreductase]]
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[[Category: Trimethyaminuria]]
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Current revision

Joint-functions of protein residues and NADP(H) in oxygen-activation by flavin-containing monooxygenase: complex with thioNADP

PDB ID 2xlu

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