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1prx

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Revision as of 09:33, 8 September 2021

HORF6 A NOVEL HUMAN PEROXIDASE ENZYME

Structural highlights

1prx is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PRDX6_HUMAN] Involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1prx"

@@ Line 3: / Line 3: @@
 <StructureSection load='1prx' size='340' side='right'caption='[[1prx]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1prx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PRX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1prx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PRX FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1prx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1prx OCA], [http://pdbe.org/1prx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1prx RCSB], [http://www.ebi.ac.uk/pdbsum/1prx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1prx ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1prx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1prx OCA], [https://pdbe.org/1prx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1prx RCSB], [https://www.ebi.ac.uk/pdbsum/1prx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1prx ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PRDX6_HUMAN PRDX6_HUMAN]] Involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.
+[[https://www.uniprot.org/uniprot/PRDX6_HUMAN PRDX6_HUMAN]] Involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1prx

From Proteopedia

Revision as of 09:33, 8 September 2021

HORF6 A NOVEL HUMAN PEROXIDASE ENZYME

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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