1h83

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{{STRUCTURE_1h83| PDB=1h83 | SCENE= }}
{{STRUCTURE_1h83| PDB=1h83 | SCENE= }}
===STRUCTURE OF POLYAMINE OXIDASE IN COMPLEX WITH 1,8-DIAMINOOCTANE===
===STRUCTURE OF POLYAMINE OXIDASE IN COMPLEX WITH 1,8-DIAMINOOCTANE===
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{{ABSTRACT_PUBMED_11258887}}
{{ABSTRACT_PUBMED_11258887}}
==About this Structure==
==About this Structure==
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1H83 is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H83 OCA].
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[[1h83]] is a 3 chain structure of [[Polyamine oxidase]] with sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H83 OCA].
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==See Also==
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*[[Polyamine oxidase|Polyamine oxidase]]
==Reference==
==Reference==
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<ref group="xtra">PMID:11258887</ref><references group="xtra"/>
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<ref group="xtra">PMID:011258887</ref><ref group="xtra">PMID:019199575</ref><references group="xtra"/>
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[[Category: Polyamine oxidase]]
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[[Category: Oxidoreductase]]
[[Category: Zea mays]]
[[Category: Zea mays]]
[[Category: Angelini, R.]]
[[Category: Angelini, R.]]
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[[Category: Flavin-dependent amine oxidase]]
[[Category: Flavin-dependent amine oxidase]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 22:37:15 2009''
 

Revision as of 06:34, 27 July 2012

Template:STRUCTURE 1h83

Contents

STRUCTURE OF POLYAMINE OXIDASE IN COMPLEX WITH 1,8-DIAMINOOCTANE

Template:ABSTRACT PUBMED 11258887

About this Structure

1h83 is a 3 chain structure of Polyamine oxidase with sequence from Zea mays. Full crystallographic information is available from OCA.

See Also

Reference

  • Binda C, Angelini R, Federico R, Ascenzi P, Mattevi A. Structural bases for inhibitor binding and catalysis in polyamine oxidase. Biochemistry. 2001 Mar 6;40(9):2766-76. PMID:11258887
  • Henderson Pozzi M, Gawandi V, Fitzpatrick PF. pH dependence of a mammalian polyamine oxidase: insights into substrate specificity and the role of lysine 315. Biochemistry. 2009 Feb 24;48(7):1508-16. PMID:19199575 doi:10.1021/bi802227m

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