Atomistry » Copper » PDB 5z86-5zpo » 5zox
Atomistry »
  Copper »
    PDB 5z86-5zpo »
      5zox »

Copper in PDB 5zox: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 7 at 288 K (1)

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 7 at 288 K (1)

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 7 at 288 K (1):
1.4.3.21;

Protein crystallography data

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 7 at 288 K (1), PDB code: 5zox was solved by T.Murakawa, S.Baba, Y.Kawano, H.Hayashi, T.Yano, K.Tanizawa, T.Kumasaka, M.Yamamoto, T.Okajima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.39 / 1.69
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 193.568, 64.390, 158.854, 90.00, 117.14, 90.00
R / Rfree (%) 19.6 / 22.7

Other elements in 5zox:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 7 at 288 K (1) also contains other interesting chemical elements:

Sodium (Na) 3 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 7 at 288 K (1) (pdb code 5zox). 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 Anaerobically Reduced By Ethylamine at pH 7 at 288 K (1), PDB code: 5zox:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5zox

Go back to Copper Binding Sites List in 5zox
Copper binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 7 at 288 K (1)


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 Anaerobically Reduced By Ethylamine at pH 7 at 288 K (1) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:21.4
occ:1.00
O A:HOH867 1.9 26.8 0.6
NE2 A:HIS431 1.9 16.4 1.0
NE2 A:HIS433 2.0 19.2 1.0
ND1 A:HIS592 2.0 19.7 1.0
O A:HOH1134 2.4 18.4 0.4
OH A:TYQ382 2.6 34.6 0.7
CE1 A:HIS431 2.9 17.6 1.0
CD2 A:HIS431 2.9 16.5 1.0
CE1 A:HIS433 3.0 20.4 1.0
CE1 A:HIS592 3.0 22.4 1.0
CG A:HIS592 3.0 18.6 1.0
CD2 A:HIS433 3.1 20.0 1.0
CB A:HIS592 3.3 16.1 1.0
CZ A:TYQ382 3.4 30.9 0.7
O A:HOH1040 3.9 33.2 0.6
N5 A:TYQ382 4.0 39.1 0.7
ND1 A:HIS431 4.0 17.2 1.0
CG A:HIS431 4.1 18.0 1.0
CE2 A:TYQ382 4.1 33.5 0.7
ND1 A:HIS433 4.1 20.3 1.0
NE2 A:HIS592 4.1 21.6 1.0
CD2 A:HIS592 4.2 19.8 1.0
CG A:HIS433 4.2 15.3 1.0
CE1 A:TYQ382 4.2 34.7 0.7
O A:HOH817 4.3 19.5 1.0
OZ A:TYQ382 4.4 32.7 0.3
CE A:MET602 4.8 27.7 0.7
SD A:MET602 4.9 32.1 0.3
CA A:HIS592 4.9 18.4 1.0
CE A:MET602 4.9 33.8 0.3
SD A:MET602 4.9 28.1 0.7

Copper binding site 2 out of 2 in 5zox

Go back to Copper Binding Sites List in 5zox
Copper binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 7 at 288 K (1)


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 Anaerobically Reduced By Ethylamine at pH 7 at 288 K (1) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu701

b:22.1
occ:1.00
NE2 B:HIS433 2.0 18.3 1.0
NE2 B:HIS431 2.0 21.2 1.0
ND1 B:HIS592 2.1 18.8 1.0
O B:HOH1013 2.1 36.3 1.0
OH B:TYQ382 2.5 35.0 0.8
O B:HOH1171 2.6 11.2 0.3
CE1 B:HIS433 3.0 20.8 1.0
CE1 B:HIS431 3.0 18.9 1.0
CE1 B:HIS592 3.0 24.4 1.0
CD2 B:HIS433 3.0 24.1 1.0
CD2 B:HIS431 3.0 13.4 1.0
CG B:HIS592 3.1 22.6 1.0
CZ B:TYQ382 3.3 26.9 0.8
CB B:HIS592 3.4 21.4 1.0
O B:HOH1186 3.8 44.3 0.2
O B:HOH1228 3.8 47.5 1.0
CE2 B:TYQ382 4.0 37.9 0.8
CE1 B:TYQ382 4.1 28.8 0.8
ND1 B:HIS433 4.1 17.3 1.0
N5 B:TYQ382 4.1 52.4 0.8
OZ B:TYQ382 4.1 34.0 0.2
ND1 B:HIS431 4.1 18.2 1.0
NE2 B:HIS592 4.2 19.2 1.0
CG B:HIS433 4.2 20.0 1.0
CG B:HIS431 4.2 15.0 1.0
CD2 B:HIS592 4.2 20.8 1.0
O B:HOH851 4.3 23.4 1.0
CA B:HIS592 4.9 18.6 1.0
SD B:MET602 4.9 30.5 1.0
CG1 B:VAL406 5.0 20.9 0.8

Reference:

T.Murakawa, S.Baba, Y.Kawano, H.Hayashi, T.Yano, T.Kumasaka, M.Yamamoto, K.Tanizawa, T.Okajima. In Crystallothermodynamic Analysis of Conformational Change of the Topaquinone Cofactor in Bacterial Copper Amine Oxidase. Proc. Natl. Acad. Sci. V. 116 135 2019U.S.A..
ISSN: ESSN 1091-6490
PubMed: 30563857
DOI: 10.1073/PNAS.1811837116
Page generated: Mon Jul 14 05:47:50 2025

Last articles

K in 2VQO
K in 2VI5
K in 2VQM
K in 2VQJ
K in 2VPL
K in 2VLH
K in 2VLF
K in 2VKP
K in 2VJJ
K in 2VGI
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy