1w2z

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[[Image:1w2z.jpg|left|200px]]<br /><applet load="1w2z" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1w2z.jpg|left|200px]]
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caption="1w2z, resolution 2.24&Aring;" />
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'''PSAO AND XENON'''<br />
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{{Structure
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|PDB= 1w2z |SIZE=350|CAPTION= <scene name='initialview01'>1w2z</scene>, resolution 2.24&Aring;
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|SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Chain+D'>AC1</scene>
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> and <scene name='pdbligand=XE:XENON'>XE</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Amine_oxidase_(copper-containing) Amine oxidase (copper-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.6 1.4.3.6]
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|GENE=
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}}
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'''PSAO AND XENON'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1W2Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=IOD:'>IOD</scene>, <scene name='pdbligand=CU:'>CU</scene> and <scene name='pdbligand=XE:'>XE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Amine_oxidase_(copper-containing) Amine oxidase (copper-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.6 1.4.3.6] Known structural/functional Site: <scene name='pdbsite=AC1:Nag+Binding+Site+For+Chain+D'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W2Z OCA].
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1W2Z is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W2Z OCA].
==Reference==
==Reference==
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Using xenon as a probe for dioxygen-binding sites in copper amine oxidases., Duff AP, Trambaiolo DM, Cohen AE, Ellis PJ, Juda GA, Shepard EM, Langley DB, Dooley DM, Freeman HC, Guss JM, J Mol Biol. 2004 Nov 26;344(3):599-607. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15533431 15533431]
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Using xenon as a probe for dioxygen-binding sites in copper amine oxidases., Duff AP, Trambaiolo DM, Cohen AE, Ellis PJ, Juda GA, Shepard EM, Langley DB, Dooley DM, Freeman HC, Guss JM, J Mol Biol. 2004 Nov 26;344(3):599-607. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15533431 15533431]
[[Category: Amine oxidase (copper-containing)]]
[[Category: Amine oxidase (copper-containing)]]
[[Category: Pisum sativum]]
[[Category: Pisum sativum]]
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[[Category: xenon]]
[[Category: xenon]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:39:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:51:23 2008''

Revision as of 12:51, 20 March 2008

Image:1w2z.jpg


PDB ID 1w2z

Drag the structure with the mouse to rotate
, resolution 2.24Å
Sites:
Ligands: , , , and
Activity: Amine oxidase (copper-containing), with EC number 1.4.3.6
Coordinates: save as pdb, mmCIF, xml



PSAO AND XENON


Overview

Potential dioxygen-binding sites in three Cu amine oxidases have been investigated by recording X-ray diffraction data at 1.7-2.2A resolution for crystals under a high pressure of xenon gas. Electron-density difference maps and crystallographic refinement provide unequivocal evidence for a number of Xe-binding sites in each enzyme. Only one of these sites is present in all three Cu amine oxidases studied. Structural changes elsewhere in the protein molecules are insignificant. The results illustrate the use of xenon as a probe for cavities, in which a protein may accommodate a dioxygen molecule. The finding of a potential dioxygen-binding cavity close to the active site of Cu amine oxidases may be relevant to the function of the enzymes, since the formation of a transient protein-dioxygen complex is a likely step in the catalytic mechanism. No evidence was found for xenon binding in a region of the molecule that was previously identified in two other Cu amine oxidases as a potential transient dioxygen-binding site.

About this Structure

1W2Z is a Single protein structure of sequence from Pisum sativum. Full crystallographic information is available from OCA.

Reference

Using xenon as a probe for dioxygen-binding sites in copper amine oxidases., Duff AP, Trambaiolo DM, Cohen AE, Ellis PJ, Juda GA, Shepard EM, Langley DB, Dooley DM, Freeman HC, Guss JM, J Mol Biol. 2004 Nov 26;344(3):599-607. PMID:15533431

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