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Copper in PDB 3x41: Copper Amine Oxidase From Arthrobacter Globiformis: Product Schiff- Base Form Produced By Anaerobic Reduction in the Presence of Sodium Bromide

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis: Product Schiff- Base Form Produced By Anaerobic Reduction in the Presence of Sodium Bromide

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis: Product Schiff- Base Form Produced By Anaerobic Reduction in the Presence of Sodium Bromide:
1.4.3.21;

Protein crystallography data

The structure of Copper Amine Oxidase From Arthrobacter Globiformis: Product Schiff- Base Form Produced By Anaerobic Reduction in the Presence of Sodium Bromide, PDB code: 3x41 was solved by T.Okajima, S.Nakanishi, T.Murakawa, M.Kataoka, H.Hayashi, A.Hamaguchi, T.Nakai, Y.Kawano, H.Yamaguchi, K.Tanizawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.88 / 1.87
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 191.619, 63.290, 157.851, 90.00, 117.21, 90.00
R / Rfree (%) 15.1 / 18

Other elements in 3x41:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis: Product Schiff- Base Form Produced By Anaerobic Reduction in the Presence of Sodium Bromide also contains other interesting chemical elements:

Potassium (K) 2 atoms
Bromine (Br) 8 atoms
Sodium (Na) 2 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Copper Amine Oxidase From Arthrobacter Globiformis: Product Schiff- Base Form Produced By Anaerobic Reduction in the Presence of Sodium Bromide (pdb code 3x41). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Copper Amine Oxidase From Arthrobacter Globiformis: Product Schiff- Base Form Produced By Anaerobic Reduction in the Presence of Sodium Bromide, PDB code: 3x41:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 3x41

Go back to Copper Binding Sites List in 3x41
Copper binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis: Product Schiff- Base Form Produced By Anaerobic Reduction in the Presence of Sodium Bromide


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Copper Amine Oxidase From Arthrobacter Globiformis: Product Schiff- Base Form Produced By Anaerobic Reduction in the Presence of Sodium Bromide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:14.7
occ:1.00
 ND1 A:HIS592 2.0 14.2 1.0
NE2 A:HIS431 2.1 16.2 1.0
NE2 A:HIS433 2.1 15.6 1.0
BR A:BR702 2.5 23.4 1.0
O A:HOH1154 2.7 36.6 1.0
CE1 A:HIS592 3.0 17.3 1.0
CE1 A:HIS431 3.0 16.6 1.0
CD2 A:HIS433 3.0 15.9 1.0
CE1 A:HIS433 3.1 17.5 1.0
CG A:HIS592 3.1 15.2 1.0
CD2 A:HIS431 3.1 13.7 1.0
CB A:HIS592 3.4 15.9 1.0
NE2 A:HIS592 4.1 15.7 1.0
ND1 A:HIS431 4.1 14.0 1.0
ND1 A:HIS433 4.2 14.2 1.0
CD2 A:HIS592 4.2 12.9 1.0
CG A:HIS433 4.2 13.4 1.0
CG A:HIS431 4.2 14.8 1.0
O A:HOH814 4.3 15.3 1.0
O A:HOH834 4.6 17.9 1.0
O A:HOH1343 4.6 43.0 1.0
OX1 A:2TY382 4.8 17.1 1.0
SD A:MET602 5.0 35.4 1.0
CA A:HIS592 5.0 15.2 1.0

Copper binding site 2 out of 2 in 3x41

Go back to Copper Binding Sites List in 3x41
Copper binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis: Product Schiff- Base Form Produced By Anaerobic Reduction in the Presence of Sodium Bromide


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Copper Amine Oxidase From Arthrobacter Globiformis: Product Schiff- Base Form Produced By Anaerobic Reduction in the Presence of Sodium Bromide within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu701

b:14.0
occ:1.00
 NE2 B:HIS433 2.0 12.2 1.0
ND1 B:HIS592 2.0 13.0 1.0
NE2 B:HIS431 2.1 15.2 1.0
BR B:BR702 2.5 22.3 1.0
O B:HOH1149 2.6 38.4 1.0
CD2 B:HIS433 3.0 12.7 1.0
CE1 B:HIS592 3.0 17.1 1.0
CE1 B:HIS431 3.0 12.3 1.0
CE1 B:HIS433 3.0 13.2 1.0
CD2 B:HIS431 3.1 14.5 1.0
CG B:HIS592 3.1 14.7 1.0
CB B:HIS592 3.4 13.5 1.0
NE2 B:HIS592 4.1 12.6 1.0
ND1 B:HIS433 4.1 12.2 1.0
CG B:HIS433 4.1 13.5 1.0
ND1 B:HIS431 4.1 14.0 1.0
CD2 B:HIS592 4.2 13.1 1.0
CG B:HIS431 4.2 14.2 1.0
O B:HOH822 4.3 12.1 1.0
O B:HOH873 4.6 16.0 1.0
OX1 B:2TY382 4.7 12.4 1.0
O B:HOH1357 4.8 33.3 1.0
CE B:MET602 4.8 35.9 1.0
CA B:HIS592 5.0 12.9 1.0

Reference:

T.Murakawa, A.Hamaguchi, S.Nakanishi, M.Kataoka, T.Nakai, Y.Kawano, H.Yamaguchi, H.Hayashi, K.Tanizawa, T.Okajima. Probing the Catalytic Mechanism of Copper Amine Oxidase From Arthrobacter Globiformis with Halide Ions J.Biol.Chem. 2015.
ISSN: ESSN 1083-351X
DOI: 10.1074/JBC.M115.662726
Page generated: Wed Jul 31 02:29:45 2024

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