3WA3: Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis in N2 Condition

Citation:
Abstract
The crystal structure of a copper amine oxidase from Arthrobacter globiformis was determined at 1.08 A resolution with the use of low-molecular-weight polyethylene glycol (LMW PEG; average molecular weight approximately 200) as a cryoprotectant. The final crystallographic R factor and Rfree were 13.0 and 15.0%, respectively. Several molecules of LMW PEG were found to occupy cavities in the protein interior, including the active site, which resulted in a marked reduction in the overall B factor and consequently led to a subatomic resolution structure for a relatively large protein with a monomer molecular weight of approximately 70 000. About 40% of the presumed H atoms were observed as clear electron densities in the Fo - Fc difference map. Multiple minor conformers were also identified for many residues. Anisotropic displacement fluctuations were evaluated in the active site, which contains a post-translationally derived quinone cofactor and a Cu atom. Furthermore, diatomic molecules, most likely to be molecular oxygen, are bound to the protein, one of which is located in a region that had previously been proposed as an entry route for the dioxygen substrate from the central cavity of the dimer interface to the active site.
PDB ID: 3WA3Download
MMDB ID: 113318
PDB Deposition Date: 2013/4/22
Updated in MMDB: 2013/09 
Experimental Method:
x-ray diffraction
Resolution: 1.55  Å
Source Organism:
Similar Structures:
Biological Unit for 3WA3: dimeric; determined by author and by software (PISA)
Molecular Components in 3WA3
Label Count Molecule
Proteins (2 molecules)
2
Phenylethylamine Oxidase
Molecule annotation
Chemicals (46 molecules)
1
2
2
2
3
6
4
4
5
2
6
16
7
12
8
2
* Click molecule labels to explore molecular sequence information.

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