1f8s: Difference between revisions

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[[Image:1f8s.png|left|200px]]
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===CRYSTAL STRUCTURE OF L-AMINO ACID OXIDASE FROM CALLOSELASMA RHODOSTOMA, COMPLEXED WITH THREE MOLECULES OF O-AMINOBENZOATE.===
===CRYSTAL STRUCTURE OF L-AMINO ACID OXIDASE FROM CALLOSELASMA RHODOSTOMA, COMPLEXED WITH THREE MOLECULES OF O-AMINOBENZOATE.===


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==About this Structure==
==About this Structure==
1F8S is a 8 chains structure of sequences from [http://en.wikipedia.org/wiki/Calloselasma_rhodostoma Calloselasma rhodostoma]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F8S OCA].  
[[1f8s]] is a 8 chain structure of [[Amino acid oxidase]] with sequence from [http://en.wikipedia.org/wiki/Calloselasma_rhodostoma Calloselasma rhodostoma]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F8S OCA].  
 
==See Also==
*[[Amino acid oxidase|Amino acid oxidase]]


==Reference==
==Reference==
<ref group="xtra">PMID:10944103</ref><references group="xtra"/>
<ref group="xtra">PMID:010944103</ref><ref group="xtra">PMID:019199575</ref><references group="xtra"/>
[[Category: Calloselasma rhodostoma]]
[[Category: Calloselasma rhodostoma]]
[[Category: L-amino-acid oxidase]]
[[Category: L-amino-acid oxidase]]
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[[Category: O-aminobenzoate]]
[[Category: O-aminobenzoate]]
[[Category: Oxidase]]
[[Category: Oxidase]]
 
[[Category: Oxidoreductase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 12:25:18 2009''

Revision as of 11:57, 25 July 2012

File:1f8s.png

Template:STRUCTURE 1f8s

CRYSTAL STRUCTURE OF L-AMINO ACID OXIDASE FROM CALLOSELASMA RHODOSTOMA, COMPLEXED WITH THREE MOLECULES OF O-AMINOBENZOATE.

Template:ABSTRACT PUBMED 10944103

About this Structure

1f8s is a 8 chain structure of Amino acid oxidase with sequence from Calloselasma rhodostoma. Full crystallographic information is available from OCA.

See Also

Reference

  1. Pawelek PD, Cheah J, Coulombe R, Macheroux P, Ghisla S, Vrielink A. The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site. EMBO J. 2000 Aug 15;19(16):4204-15. PMID:10944103 doi:10.1093/emboj/19.16.4204
  2. 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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