Atomistry » Copper » PDB 3x2q-4b5q » 3x41
Atomistry »
  Copper »
    PDB 3x2q-4b5q »
      3x41 »

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

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy