2j18: Difference between revisions

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<StructureSection load='2j18' size='340' side='right' caption='[[2j18]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='2j18' size='340' side='right' caption='[[2j18]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2j18]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Leptoxyphium_fumago Leptoxyphium fumago]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J18 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2J18 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2j18]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Calfu Calfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J18 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2J18 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cpo|1cpo]], [[2civ|2civ]], [[2ciw|2ciw]], [[2cix|2cix]], [[2ciy|2ciy]], [[2ciz|2ciz]], [[2cj0|2cj0]], [[2cj1|2cj1]], [[2cj2|2cj2]], [[2cpo|2cpo]], [[2j19|2j19]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cpo|1cpo]], [[2civ|2civ]], [[2ciw|2ciw]], [[2cix|2cix]], [[2ciy|2ciy]], [[2ciz|2ciz]], [[2cj0|2cj0]], [[2cj1|2cj1]], [[2cj2|2cj2]], [[2cpo|2cpo]], [[2j19|2j19]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chloride_peroxidase Chloride peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.10 1.11.1.10] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chloride_peroxidase Chloride peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.10 1.11.1.10] </span></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=2j18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j18 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2j18 RCSB], [http://www.ebi.ac.uk/pdbsum/2j18 PDBsum]</span></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=2j18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j18 OCA], [http://pdbe.org/2j18 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j18 RCSB], [http://www.ebi.ac.uk/pdbsum/2j18 PDBsum]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 2j18" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Calfu]]
[[Category: Chloride peroxidase]]
[[Category: Chloride peroxidase]]
[[Category: Leptoxyphium fumago]]
[[Category: Beitlich, T]]
[[Category: Beitlich, T]]
[[Category: Kuhnel, K]]
[[Category: Kuhnel, K]]

Revision as of 17:55, 11 September 2015

CHLOROPEROXIDASE MIXTURE OF FERRIC AND FERROUS STATES (LOW DOSE DATA SET)CHLOROPEROXIDASE MIXTURE OF FERRIC AND FERROUS STATES (LOW DOSE DATA SET)

Structural highlights

2j18 is a 1 chain structure with sequence from Calfu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , ,
NonStd Res:
Activity:Chloride peroxidase, with EC number 1.11.1.10
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

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

The X-ray crystallographic analysis of redox-active systems may be complicated by photoreduction. Although radiolytic reduction by the probing X-ray beam may be exploited to generate otherwise short-lived reaction intermediates of metalloproteins, it is generally an undesired feature. Here, the X-ray-induced reduction of the three heme proteins myoglobin, cytochrome P450cam and chloroperoxidase has been followed by on-line UV-Vis absorption spectroscopy. All three systems showed a very rapid reduction of the heme iron. In chloroperoxidase the change of the ionization state from ferric to ferrous heme is associated with a movement of the heme-coordinating water molecule. The influence of the energy of the incident X-ray photons and of the presence of scavengers on the apparent reduction rate of ferric myoglobin crystals was analyzed.

Cryoradiolytic reduction of crystalline heme proteins: analysis by UV-Vis spectroscopy and X-ray crystallography.,Beitlich T, Kuhnel K, Schulze-Briese C, Shoeman RL, Schlichting I J Synchrotron Radiat. 2007 Jan;14(Pt 1):11-23. Epub 2006 Dec 15. PMID:17211068[1]

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

References

  1. Beitlich T, Kuhnel K, Schulze-Briese C, Shoeman RL, Schlichting I. Cryoradiolytic reduction of crystalline heme proteins: analysis by UV-Vis spectroscopy and X-ray crystallography. J Synchrotron Radiat. 2007 Jan;14(Pt 1):11-23. Epub 2006 Dec 15. PMID:17211068 doi:10.1107/S0909049506049806

2j18, resolution 1.75Å

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OCA