3pah
From Proteopedia
(New page: 200px<br /> <applet load="3pah" size="450" color="white" frame="true" align="right" spinBox="true" caption="3pah, resolution 2.0Å" /> '''HUMAN PHENYLALANINE ...) |
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==About this Structure== | ==About this Structure== | ||
| - | 3PAH is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with FE and ALE as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.16.1 1.14.16.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3PAH OCA]]. | + | 3PAH is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with FE and ALE as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Phenylalanine_4-monooxygenase Phenylalanine 4-monooxygenase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.16.1 1.14.16.1]]. Structure known Active Site: NUL. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3PAH OCA]]. |
==Reference== | ==Reference== | ||
Crystallographic analysis of the human phenylalanine hydroxylase catalytic domain with bound catechol inhibitors at 2.0 A resolution., Erlandsen H, Flatmark T, Stevens RC, Hough E, Biochemistry. 1998 Nov 10;37(45):15638-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9843368 9843368] | Crystallographic analysis of the human phenylalanine hydroxylase catalytic domain with bound catechol inhibitors at 2.0 A resolution., Erlandsen H, Flatmark T, Stevens RC, Hough E, Biochemistry. 1998 Nov 10;37(45):15638-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9843368 9843368] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| + | [[Category: Phenylalanine 4-monooxygenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Erlandsen, H.]] | [[Category: Erlandsen, H.]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:20:37 2007'' |
Revision as of 10:15, 30 October 2007
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HUMAN PHENYLALANINE HYDROXYLASE CATALYTIC DOMAIN DIMER WITH BOUND ADRENALINE INHIBITOR
Overview
The aromatic amino acid hydroxylases represent a superfamily of, structurally and functionally closely related enzymes, one of those, functions being reversible inhibition by catechol derivatives. Here we, present the crystal structure of the dimeric catalytic domain (residues, 117-424) of human phenylalanine hydroxylase (hPheOH), cocrystallized with, various potent and well-known catechol inhibitors and refined at a, resolution of 2.0 A. The catechols bind by bidentate coordination to each, iron in both subunits of the dimer through the catechol hydroxyl groups, forming a blue-green colored ligand-to-metal charge-transfer complex. In, addition, Glu330 and Tyr325 are identified as determinant residues in the, recognition of the inhibitors. In particular, the interaction with Glu330, ... [(full description)]
About this Structure
3PAH is a [Single protein] structure of sequence from [Homo sapiens] with FE and ALE as [ligands]. Active as [Phenylalanine 4-monooxygenase], with EC number [1.14.16.1]. Structure known Active Site: NUL. Full crystallographic information is available from [OCA].
Reference
Crystallographic analysis of the human phenylalanine hydroxylase catalytic domain with bound catechol inhibitors at 2.0 A resolution., Erlandsen H, Flatmark T, Stevens RC, Hough E, Biochemistry. 1998 Nov 10;37(45):15638-46. PMID:9843368
Page seeded by OCA on Tue Oct 30 12:20:37 2007
