2xlu
From Proteopedia
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==JOINT-FUNCTIONS OF PROTEIN RESIDUES AND NADP(H) IN OXYGEN-ACTIVATION BY FLAVIN-CONTAINING MONOOXYGENASE: COMPLEX WITH THIONADP== | ==JOINT-FUNCTIONS OF PROTEIN RESIDUES AND NADP(H) IN OXYGEN-ACTIVATION BY FLAVIN-CONTAINING MONOOXYGENASE: COMPLEX WITH THIONADP== | ||
<StructureSection load='2xlu' size='340' side='right' caption='[[2xlu]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='2xlu' size='340' side='right' caption='[[2xlu]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2xlu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <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> |
</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> | </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> | ||
<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> | <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> | ||
<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> | <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> | ||
| - | <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://www.rcsb.org/pdb/explore.do?structureId=2xlu RCSB], [http://www.ebi.ac.uk/pdbsum/2xlu 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=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> |
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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<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/ | + | </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=2xlu ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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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 2xlu" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Flavin-containing monooxygenase]] | [[Category: Flavin-containing monooxygenase]] | ||
| - | [[Category: | + | [[Category: Jcm 14647]] |
[[Category: Fraaije, M W]] | [[Category: Fraaije, M W]] | ||
[[Category: Mattevi, A]] | [[Category: Mattevi, A]] | ||
Revision as of 17:51, 5 August 2016
JOINT-FUNCTIONS OF PROTEIN RESIDUES AND NADP(H) IN OXYGEN-ACTIVATION BY FLAVIN-CONTAINING MONOOXYGENASE: COMPLEX WITH THIONADP
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