1d6u
From Proteopedia
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|PDB= 1d6u |SIZE=350|CAPTION= <scene name='initialview01'>1d6u</scene>, resolution 2.4Å | |PDB= 1d6u |SIZE=350|CAPTION= <scene name='initialview01'>1d6u</scene>, resolution 2.4Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HY1:PHENYLACETALDEHYDE'>HY1</scene>, <scene name='pdbligand=PEA:2-PHENYLETHYLAMINE'>PEA</scene>, <scene name='pdbligand=TYQ:3-AMINO-6-HYDROXY-TYROSINE'>TYQ</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=[[1oac|1OAC]], [[1spu|1SPU]], [[1jez|1JEZ]], [[1qaf|1QAF]], [[1qak|1QAK]], [[1qal|1QAL]], [[1d6u|1D6U]], [[1d6y|1D6Y]], [[1d6z|1D6Z]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d6u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d6u OCA], [http://www.ebi.ac.uk/pdbsum/1d6u PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d6u RCSB]</span> | ||
}} | }} | ||
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[[Category: Phillips, S E.V.]] | [[Category: Phillips, S E.V.]] | ||
[[Category: Wilmot, C M.]] | [[Category: Wilmot, C M.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: CU]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: HY1]] | ||
| - | [[Category: PEA]] | ||
[[Category: reaction intermediate]] | [[Category: reaction intermediate]] | ||
| - | ''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 19:35:49 2008'' |
Revision as of 16:35, 30 March 2008
| |||||||
| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , | ||||||
| Activity: | Amine oxidase (copper-containing), with EC number 1.4.3.6 | ||||||
| Related: | 1OAC, 1SPU, 1JEZ, 1QAF, 1QAK, 1QAL, 1D6U, 1D6Y, 1D6Z
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF E. COLI AMINE OXIDASE ANAEROBICALLY REDUCED WITH BETA-PHENYLETHYLAMINE
Overview
X-ray crystal structures of three species related to the oxidative half of the reaction of the copper-containing quinoprotein amine oxidase from Escherichia coli have been determined. Crystals were freeze-trapped either anaerobically or aerobically after exposure to substrate, and structures were determined to resolutions between 2.1 and 2.4 angstroms. The oxidation state of the quinone cofactor was investigated by single-crystal spectrophotometry. The structures reveal the site of bound dioxygen and the proton transfer pathways involved in oxygen reduction. The quinone cofactor is regenerated from the iminoquinone intermediate by hydrolysis involving Asp383, the catalytic base in the reductive half-reaction. Product aldehyde inhibits the hydrolysis, making release of product the rate-determining step of the reaction in the crystal.
About this Structure
1D6U is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Visualization of dioxygen bound to copper during enzyme catalysis., Wilmot CM, Hajdu J, McPherson MJ, Knowles PF, Phillips SE, Science. 1999 Nov 26;286(5445):1724-8. PMID:10576737
Page seeded by OCA on Sun Mar 30 19:35:49 2008
