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1prx

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[[Image:1prx.gif|left|200px]]<br /><applet load="1prx" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1prx.gif|left|200px]]
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caption="1prx, resolution 2.0&Aring;" />
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'''HORF6 A NOVEL HUMAN PEROXIDASE ENZYME'''<br />
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{{Structure
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|PDB= 1prx |SIZE=350|CAPTION= <scene name='initialview01'>1prx</scene>, resolution 2.0&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE=
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}}
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'''HORF6 A NOVEL HUMAN PEROXIDASE ENZYME'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1PRX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRX OCA].
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1PRX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRX OCA].
==Reference==
==Reference==
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Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution., Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE, Nat Struct Biol. 1998 May;5(5):400-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9587003 9587003]
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Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution., Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE, Nat Struct Biol. 1998 May;5(5):400-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9587003 9587003]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: redox regulation]]
[[Category: redox regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:31:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:28:10 2008''

Revision as of 11:28, 20 March 2008


PDB ID 1prx

Drag the structure with the mouse to rotate
, resolution 2.0Å
Coordinates: save as pdb, mmCIF, xml



HORF6 A NOVEL HUMAN PEROXIDASE ENZYME


Overview

Hydrogen peroxide (H2O2) has been implicated recently as an intracellular messenger that affects cellular processes including protein phosphorylation, transcription and apoptosis. A set of novel peroxidases, named peroxiredoxins (Prx), regulate the intracellular concentration of H2O2 by reducing it in the presence of an appropriate electron donor. The crystal structure of a human Prx enzyme, hORF6, reveals that the protein contains two discrete domains and forms a dimer. The N-terminal domain has a thioredoxin fold and the C-terminal domain is used for dimerization. The active site cysteine (Cys 47), which exists as cysteine-sulfenic acid in the crystal, is located at the bottom of a relatively narrow pocket. The positively charged environment surrounding Cys 47 accounts for the peroxidase activity of the enzyme, which contains no redox cofactors.

About this Structure

1PRX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution., Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE, Nat Struct Biol. 1998 May;5(5):400-6. PMID:9587003

Page seeded by OCA on Thu Mar 20 13:28:10 2008

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