1prx
From Proteopedia
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| - | [[Image:1prx.gif|left|200px]] | + | [[Image:1prx.gif|left|200px]] |
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| - | '''HORF6 A NOVEL HUMAN PEROXIDASE ENZYME''' | + | {{Structure |
| + | |PDB= 1prx |SIZE=350|CAPTION= <scene name='initialview01'>1prx</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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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== | ||
| - | 1PRX is a [ | + | 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== | ||
| - | 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:// | + | 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]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''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
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| 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
