1iuw

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[[Image:1iuw.png|left|200px]]
[[Image:1iuw.png|left|200px]]
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{{STRUCTURE_1iuw| PDB=1iuw | SCENE= }}
{{STRUCTURE_1iuw| PDB=1iuw | SCENE= }}
===P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-4-HYDROXYBENZOATE AT PH 7.4===
===P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-4-HYDROXYBENZOATE AT PH 7.4===
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{{ABSTRACT_PUBMED_8555229}}
{{ABSTRACT_PUBMED_8555229}}
==About this Structure==
==About this Structure==
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1IUW is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_pao1 Pseudomonas aeruginosa pao1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IUW OCA].
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[[1iuw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IUW OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:8555229</ref><references group="xtra"/>
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<ref group="xtra">PMID:008555229</ref><references group="xtra"/>
[[Category: 4-hydroxybenzoate 3-monooxygenase]]
[[Category: 4-hydroxybenzoate 3-monooxygenase]]
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[[Category: Pseudomonas aeruginosa pao1]]
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[[Category: Pseudomonas aeruginosa]]
[[Category: Ballou, D P.]]
[[Category: Ballou, D P.]]
[[Category: Entsch, B.]]
[[Category: Entsch, B.]]
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[[Category: Aromatic hydrocarbons catabolism]]
[[Category: Aromatic hydrocarbons catabolism]]
[[Category: Oxidoreducatase]]
[[Category: Oxidoreducatase]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 06:22:45 2009''
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Revision as of 15:06, 28 November 2012

Template:STRUCTURE 1iuw

P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-4-HYDROXYBENZOATE AT PH 7.4

Template:ABSTRACT PUBMED 8555229

About this Structure

1iuw is a 1 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

Reference

  • Gatti DL, Entsch B, Ballou DP, Ludwig ML. pH-dependent structural changes in the active site of p-hydroxybenzoate hydroxylase point to the importance of proton and water movements during catalysis. Biochemistry. 1996 Jan 16;35(2):567-78. PMID:8555229 doi:http://dx.doi.org/10.1021/bi951344i

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