1pn0

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(New page: 200px<br /><applet load="1pn0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pn0, resolution 1.70&Aring;" /> '''Phenol hydroxylase f...)
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[[Image:1pn0.jpg|left|200px]]<br /><applet load="1pn0" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1pn0, resolution 1.70&Aring;" />
caption="1pn0, resolution 1.70&Aring;" />
'''Phenol hydroxylase from Trichosporon cutaneum'''<br />
'''Phenol hydroxylase from Trichosporon cutaneum'''<br />
==Overview==
==Overview==
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The 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.
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The 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.
==About this Structure==
==About this Structure==
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1PN0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Trichosporon_cutaneum Trichosporon cutaneum] with CL, FAD and IPH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PN0 OCA].
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1PN0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Trichosporon_cutaneum Trichosporon cutaneum] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=IPH:'>IPH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PN0 OCA].
==Reference==
==Reference==
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[[Category: two dimers]]
[[Category: two dimers]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:56:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:30:24 2008''

Revision as of 12:30, 21 February 2008


1pn0, resolution 1.70Å

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Phenol hydroxylase from Trichosporon cutaneum

Overview

The 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.

About this Structure

1PN0 is a Single protein structure of sequence from Trichosporon cutaneum with , and as ligands. Active as Phenol 2-monooxygenase, with EC number 1.14.13.7 Full crystallographic information is available from OCA.

Reference

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

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