1rky
From Proteopedia
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|PDB= 1rky |SIZE=350|CAPTION= <scene name='initialview01'>1rky</scene>, resolution 1.68Å | |PDB= 1rky |SIZE=350|CAPTION= <scene name='initialview01'>1rky</scene>, resolution 1.68Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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/Protein-lysine_6-oxidase Protein-lysine 6-oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.13 1.4.3.13] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-lysine_6-oxidase Protein-lysine 6-oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.13 1.4.3.13] </span> |
|GENE= ATCC 28, 485 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4922 Pichia pastoris]) | |GENE= ATCC 28, 485 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4922 Pichia pastoris]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1n9e|1N9E]], [[1rjo|1RJO]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rky OCA], [http://www.ebi.ac.uk/pdbsum/1rky PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rky RCSB]</span> | ||
}} | }} | ||
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[[Category: Duff, A P.]] | [[Category: Duff, A P.]] | ||
[[Category: Guss, J M.]] | [[Category: Guss, J M.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: CU]] | ||
| - | [[Category: IMD]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: XE]] | ||
[[Category: amine oxidase]] | [[Category: amine oxidase]] | ||
[[Category: cao]] | [[Category: cao]] | ||
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[[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 Sun Mar 30 23:29:38 2008'' |
Revision as of 20:29, 30 March 2008
| |||||||
| , resolution 1.68Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , , , , | ||||||
| Gene: | ATCC 28, 485 (Pichia pastoris) | ||||||
| Activity: | Protein-lysine 6-oxidase, with EC number 1.4.3.13 | ||||||
| Related: | 1N9E, 1RJO
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PPLO + Xe
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
1RKY is a Single protein structure of sequence from Pichia pastoris. 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 Sun Mar 30 23:29:38 2008
