1pn0: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1pn0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Trichosporon_cutaneum Trichosporon cutaneum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PN0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PN0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1pn0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Trichosporon_cutaneum Trichosporon cutaneum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PN0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PN0 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=IPH:PHENOL'>IPH</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=IPH:PHENOL'>IPH</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1foh|1foh]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1foh|1foh]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phenol_2-monooxygenase Phenol 2-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.7 1.14.13.7] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phenol_2-monooxygenase Phenol 2-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.7 1.14.13.7] </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=1pn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pn0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pn0 RCSB], [http://www.ebi.ac.uk/pdbsum/1pn0 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=1pn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pn0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pn0 RCSB], [http://www.ebi.ac.uk/pdbsum/1pn0 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/PH2M_TRICU PH2M_TRICU]] Hydroxylates phenol to catechol. Phenol is the best substrate, but the enzyme also accepts simple hydroxyl-, amino-, halogen- or methyl-substituted phenols. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Phenol 2-monooxygenase]] | [[Category: Phenol 2-monooxygenase]] | ||
[[Category: Trichosporon cutaneum]] | [[Category: Trichosporon cutaneum]] | ||
[[Category: Enroth, C | [[Category: Enroth, C]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Tls refinement]] | [[Category: Tls refinement]] | ||
[[Category: Two dimer]] | [[Category: Two dimer]] | ||
Revision as of 06:33, 25 December 2014
Phenol hydroxylase from Trichosporon cutaneumPhenol hydroxylase from Trichosporon cutaneum
Structural highlights
Function[PH2M_TRICU] Hydroxylates phenol to catechol. Phenol is the best substrate, but the enzyme also accepts simple hydroxyl-, amino-, halogen- or methyl-substituted phenols. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure model of phenol hydroxylase has been corrected for 11 sequence errors and refined against new data to 1.7 A resolution. The higher resolution data together with careful exploitation of non-crystallographic symmetry restraints and the use of many small groups for refinement of anisotropic displacement parameters resulted in a large decrease in the crystallographic R factor. The final crystallographic free R factor is 18.0%, which should be compared with the values of 27.8% for the previously published model (PDB code 1foh). The rebuilding and re-refinement procedure is described. A comparison with the previously published model was performed and possible biochemical implications are discussed. No large differences suggesting gross errors in the earlier model were found. The actual differences between these two models give an indication of the level of ambiguity and inaccuracy that may be found in a well refined protein model at 2.4 A resolution. High-resolution structure of phenol hydroxylase and correction of sequence errors.,Enroth C Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1597-602. Epub 2003, Aug 19. PMID:12925790[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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