1w2z
From Proteopedia
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| |PDB= 1w2z |SIZE=350|CAPTION= <scene name='initialview01'>1w2z</scene>, resolution 2.24Å | |PDB= 1w2z |SIZE=350|CAPTION= <scene name='initialview01'>1w2z</scene>, resolution 2.24Å | ||
| |SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Chain+D'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Chain+D'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TPQ:5-(2-CARBOXY-2-AMINOETHYL)-2-HYDROXY-1,4-BENZOQUINONE'>TPQ</scene>, <scene name='pdbligand=XE:XENON'>XE</scene> | 
| - | |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]  | + | |ACTIVITY= <span class='plainlinks'>[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] </span> | 
| |GENE=  | |GENE=  | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w2z OCA], [http://www.ebi.ac.uk/pdbsum/1w2z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w2z RCSB]</span> | ||
| }} | }} | ||
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| [[Category: Shepard, E M.]] | [[Category: Shepard, E M.]] | ||
| [[Category: Trambaiolo, D M.]] | [[Category: Trambaiolo, D M.]] | ||
| - | [[Category: CU]] | ||
| - | [[Category: IOD]] | ||
| - | [[Category: MN]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: XE]] | ||
| [[Category: copper]] | [[Category: copper]] | ||
| [[Category: copper amine]] | [[Category: copper amine]] | ||
| Line 47: | Line 45: | ||
| [[Category: pea seedling]] | [[Category: pea seedling]] | ||
| [[Category: quinone]] | [[Category: quinone]] | ||
| - | [[Category: signal | + | [[Category: signal,tpq oxidoreductase]] | 
| - | + | ||
| [[Category: xenon]] | [[Category: xenon]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on  | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:30:25 2008'' | 
Revision as of 21:30, 30 March 2008
 
| 
 | |||||||
| , resolution 2.24Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , , , | ||||||
| Activity: | Amine oxidase (copper-containing), with EC number 1.4.3.6 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Mon Mar 31 00:30:25 2008
Categories: Amine oxidase (copper-containing) | Pisum sativum | Single protein | Cohen, A E. | Dooley, D M. | Duff, A P. | Ellis, P J. | Freeman, H C. | Guss, J M. | Juda, G A. | Langley, D B. | Shepard, E M. | Trambaiolo, D M. | Copper | Copper amine | Glycoprotein | Manganese | Metal-binding oxidase | Oxidase | Oxidoreductase | Pea seedling | Quinone | Signal,tpq oxidoreductase | Xenon
