2ckf
From Proteopedia
(Difference between revisions)
Line 3: | Line 3: | ||
<StructureSection load='2ckf' size='340' side='right'caption='[[2ckf]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='2ckf' size='340' side='right'caption='[[2ckf]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2ckf]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingomonas_sp. | + | <table><tr><td colspan='2'>[[2ckf]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingomonas_sp._CHY-1 Sphingomonas sp. CHY-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CKF FirstGlance]. <br> |
- | </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=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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]] 1.85Å</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=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></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=2ckf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ckf OCA], [https://pdbe.org/2ckf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ckf RCSB], [https://www.ebi.ac.uk/pdbsum/2ckf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ckf 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=2ckf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ckf OCA], [https://pdbe.org/2ckf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ckf RCSB], [https://www.ebi.ac.uk/pdbsum/2ckf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ckf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/Q65AT1_9SPHN Q65AT1_9SPHN] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Line 17: | Line 20: | ||
</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=2ckf 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=2ckf ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Ring-hydroxylating dioxygenases are multicomponent bacterial enzymes that catalyze the first step in the oxidative degradation of aromatic hydrocarbons. The dioxygenase from Sphingomonas CHY-1 is unique in that it can oxidize a wide range of polycyclic aromatic hydrocarbons (PAHs). With a crystal structure similar to that of the seven other known dioxygenases, its catalytic domain features the largest hydrophobic substrate binding cavity characterized so far. Molecular modeling studies indicated that the catalytic cavity is large enough to accommodate a five-ring benzo[a]pyrene molecule. The predicted positions of this and other PAHs in the substrate binding pocket are consistent with the product regio- and stereo-selectivity of the enzyme. | ||
- | + | ==See Also== | |
- | + | *[[Dioxygenase 3D structures|Dioxygenase 3D structures]] | |
- | + | ||
- | + | ||
- | + | ||
- | == | + | |
- | + | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Sphingomonas sp. | + | [[Category: Sphingomonas sp. CHY-1]] |
- | [[Category: Jakoncic | + | [[Category: Jakoncic J]] |
- | [[Category: Jouanneau | + | [[Category: Jouanneau Y]] |
- | [[Category: Meyer | + | [[Category: Meyer C]] |
- | [[Category: Stojanoff | + | [[Category: Stojanoff V]] |
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + |
Current revision
Crystal Structure of the Terminal Component of the PAH-hydroxylating Dioxygenase from Sphingomonas sp CHY-1
|