1dii: Difference between revisions

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[[Image:1dii.gif|left|200px]]<br /><applet load="1dii" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1dii.gif|left|200px]]
caption="1dii, resolution 2.5&Aring;" />
 
'''CRYSTAL STRUCTURE OF P-CRESOL METHYLHYDROXYLASE AT 2.5 A RESOLUTION'''<br />
{{Structure
|PDB= 1dii |SIZE=350|CAPTION= <scene name='initialview01'>1dii</scene>, resolution 2.5&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/4-cresol_dehydrogenase_(hydroxylating) 4-cresol dehydrogenase (hydroxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.99.1 1.17.99.1]
|GENE=
}}
 
'''CRYSTAL STRUCTURE OF P-CRESOL METHYLHYDROXYLASE AT 2.5 A RESOLUTION'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1DII is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/4-cresol_dehydrogenase_(hydroxylating) 4-cresol dehydrogenase (hydroxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.99.1 1.17.99.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DII OCA].  
1DII is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DII OCA].  


==Reference==
==Reference==
Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: gated substrate entry and proton relays support the proposed catalytic mechanism., Cunane LM, Chen ZW, Shamala N, Mathews FS, Cronin CN, McIntire WS, J Mol Biol. 2000 Jan 14;295(2):357-74. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10623531 10623531]
Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: gated substrate entry and proton relays support the proposed catalytic mechanism., Cunane LM, Chen ZW, Shamala N, Mathews FS, Cronin CN, McIntire WS, J Mol Biol. 2000 Jan 14;295(2):357-74. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10623531 10623531]
[[Category: 4-cresol dehydrogenase (hydroxylating)]]
[[Category: 4-cresol dehydrogenase (hydroxylating)]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: heme]]
[[Category: heme]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:16:53 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:38:56 2008''
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