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Copper in PDB 3x40: Copper Amine Oxidase From Arthrobacter Globiformis: Product Schiff- Base Form Produced By Anaerobic Reduction in the Presence of Sodium Chloride

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

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis: Product Schiff- Base Form Produced By Anaerobic Reduction in the Presence of Sodium Chloride:
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 Chloride, PDB code: 3x40 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) 26.22 / 1.85
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 191.812, 63.020, 158.108, 90.00, 117.29, 90.00
R / Rfree (%) 21.2 / 26.4

Other elements in 3x40:

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

Chlorine (Cl) 5 atoms
Sodium (Na) 3 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 Chloride (pdb code 3x40). 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 Chloride, PDB code: 3x40:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 3x40

Go back to Copper Binding Sites List in 3x40
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 Chloride


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 Chloride within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:15.2
occ:1.00
 O A:HOH1370 1.5 20.0 1.0
NE2 A:HIS431 2.0 23.6 1.0
NE2 A:HIS433 2.0 24.4 1.0
ND1 A:HIS592 2.1 20.7 1.0
CL A:CL702 2.3 19.4 1.0
CD2 A:HIS431 2.8 21.1 1.0
CE1 A:HIS433 2.9 18.0 1.0
CE1 A:HIS592 3.1 22.7 1.0
CE1 A:HIS431 3.1 14.3 1.0
CD2 A:HIS433 3.1 17.6 1.0
CG A:HIS592 3.1 25.4 1.0
CB A:HIS592 3.5 13.6 1.0
CG A:HIS431 4.0 21.8 1.0
ND1 A:HIS433 4.0 20.6 1.0
ND1 A:HIS431 4.1 17.3 1.0
CG A:HIS433 4.2 15.0 1.0
NE2 A:HIS592 4.2 22.4 1.0
CD2 A:HIS592 4.2 23.4 1.0
O A:HOH824 4.3 21.0 1.0
O A:HOH809 4.4 15.3 1.0
O A:HOH1295 4.7 31.9 1.0
OX1 A:2TY382 4.7 14.5 1.0
CA A:HIS592 5.0 14.0 1.0

Copper binding site 2 out of 2 in 3x40

Go back to Copper Binding Sites List in 3x40
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 Chloride


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 Chloride within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu701

b:13.7
occ:1.00
 O B:HOH1319 1.5 14.3 1.0
NE2 B:HIS431 2.0 12.2 1.0
ND1 B:HIS592 2.1 16.4 1.0
NE2 B:HIS433 2.1 15.5 1.0
CL B:CL702 2.2 22.1 1.0
CE1 B:HIS431 2.8 18.8 1.0
CE1 B:HIS592 3.0 19.2 1.0
CE1 B:HIS433 3.0 13.2 1.0
CD2 B:HIS431 3.1 11.2 1.0
CD2 B:HIS433 3.1 21.7 1.0
CG B:HIS592 3.1 21.9 1.0
CB B:HIS592 3.5 16.5 1.0
ND1 B:HIS431 4.0 11.7 1.0
NE2 B:HIS592 4.1 19.8 1.0
CG B:HIS431 4.1 13.6 1.0
ND1 B:HIS433 4.1 12.2 1.0
CD2 B:HIS592 4.2 19.6 1.0
CG B:HIS433 4.2 18.0 1.0
O B:HOH1309 4.4 12.6 1.0
O B:HOH817 4.4 11.2 1.0
O B:HOH1436 4.5 42.2 1.0
OX1 B:2TY382 4.8 11.8 1.0
CE B:MET602 4.9 11.6 1.0
SD B:MET602 4.9 32.0 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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