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==CRYSTAL STRUCTURE OF PROTOCATECHUATE 3,4-DIOXYGENASE FROM ACINETOBACTER SP. ADP1 MUTANT R133H==
 
<StructureSection load='2bux' size='340' side='right' caption='[[2bux]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
==Crystal Structure of Protocatechuate 3,4-Dioxygenase from Acinetobacter Sp. ADP1 Mutant R133H==
<StructureSection load='2bux' size='340' side='right'caption='[[2bux]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2bux]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Acinetobacter_calcoaceticus Acinetobacter calcoaceticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BUX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BUX FirstGlance]. <br>
<table><tr><td colspan='2'>[[2bux]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baylyi_ADP1 Acinetobacter baylyi ADP1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BUX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BUX FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</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]] 1.8&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1eo2|1eo2]], [[1eo9|1eo9]], [[1eoa|1eoa]], [[1eob|1eob]], [[1eoc|1eoc]], [[2bum|2bum]], [[2buq|2buq]], [[2bur|2bur]], [[2but|2but]], [[2buu|2buu]], [[2buv|2buv]], [[2buw|2buw]], [[2buy|2buy]], [[2buz|2buz]], [[2bv0|2bv0]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene></td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protocatechuate_3,4-dioxygenase Protocatechuate 3,4-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.3 1.13.11.3] </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=2bux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bux OCA], [https://pdbe.org/2bux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bux RCSB], [https://www.ebi.ac.uk/pdbsum/2bux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bux 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=2bux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bux OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bux RCSB], [http://www.ebi.ac.uk/pdbsum/2bux PDBsum]</span></td></tr>
</table>
<table>
== Function ==
[https://www.uniprot.org/uniprot/PCXA_ACIAD PCXA_ACIAD] Plays an essential role in the utilization of numerous aromatic and hydroaromatic compounds via the beta-ketoadipate pathway.
== 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/bu/2bux_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bu/2bux_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>
   </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=2bux ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Dioxygenase|Dioxygenase]]
*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Acinetobacter calcoaceticus]]
[[Category: Acinetobacter baylyi ADP1]]
[[Category: Protocatechuate 3,4-dioxygenase]]
[[Category: Large Structures]]
[[Category: Argenio, D A.D.]]
[[Category: D'Argenio DA]]
[[Category: Lipscomb, J D.]]
[[Category: Lipscomb JD]]
[[Category: Ohlendorf, D H.]]
[[Category: Ohlendorf DH]]
[[Category: Ornston, L N.]]
[[Category: Ornston LN]]
[[Category: Valley, M P.]]
[[Category: Valley MP]]
[[Category: Vetting, M W.]]
[[Category: Vetting MW]]
[[Category: Aromatic degradation]]
[[Category: Aromatic hydrocarbons catabolism]]
[[Category: Dioxygenase]]
[[Category: Iron]]
[[Category: Metal-binding]]
[[Category: Non-heme iron]]
[[Category: Oxidoreductase]]

Latest revision as of 16:56, 13 December 2023

Crystal Structure of Protocatechuate 3,4-Dioxygenase from Acinetobacter Sp. ADP1 Mutant R133HCrystal Structure of Protocatechuate 3,4-Dioxygenase from Acinetobacter Sp. ADP1 Mutant R133H

Structural highlights

2bux is a 2 chain structure with sequence from Acinetobacter baylyi ADP1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PCXA_ACIAD Plays an essential role in the utilization of numerous aromatic and hydroaromatic compounds via the beta-ketoadipate pathway.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2bux, resolution 1.80Å

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