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Atomistry » Copper » PDB 7s1d-7xma » 7wis » |
Copper in PDB 7wis: Catalytic Intermediate Structure of N381A Mutant of Copper Amine Oxidase From Arthrobacter GlobiformisEnzymatic activity of Catalytic Intermediate Structure of N381A Mutant of Copper Amine Oxidase From Arthrobacter Globiformis
All present enzymatic activity of Catalytic Intermediate Structure of N381A Mutant of Copper Amine Oxidase From Arthrobacter Globiformis:
1.4.3.21; Protein crystallography data
The structure of Catalytic Intermediate Structure of N381A Mutant of Copper Amine Oxidase From Arthrobacter Globiformis, PDB code: 7wis
was solved by
T.Murakawa,
T.Okajima,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Copper Binding Sites:
The binding sites of Copper atom in the Catalytic Intermediate Structure of N381A Mutant of Copper Amine Oxidase From Arthrobacter Globiformis
(pdb code 7wis). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Catalytic Intermediate Structure of N381A Mutant of Copper Amine Oxidase From Arthrobacter Globiformis, PDB code: 7wis: Jump to Copper binding site number: 1; 2; Copper binding site 1 out of 2 in 7wisGo back to Copper Binding Sites List in 7wis
Copper binding site 1 out
of 2 in the Catalytic Intermediate Structure of N381A Mutant of Copper Amine Oxidase From Arthrobacter Globiformis
Mono view Stereo pair view
Copper binding site 2 out of 2 in 7wisGo back to Copper Binding Sites List in 7wis
Copper binding site 2 out
of 2 in the Catalytic Intermediate Structure of N381A Mutant of Copper Amine Oxidase From Arthrobacter Globiformis
Mono view Stereo pair view
Reference:
M.Shoji,
T.Murakawa,
S.Nakanishi,
M.Boero,
Y.Shigeta,
H.Hayashi,
T.Okajima.
Molecular Mechanism of A Large Conformational Change of the Quinone Cofactor in the Semiquinone Intermediate of Bacterial Copper Amine Oxidase. Chem Sci V. 13 10923 2022.
Page generated: Tue Apr 4 23:29:49 2023
ISSN: ISSN 2041-6520 PubMed: 36320691 DOI: 10.1039/D2SC01356H |
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