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Copper in PDB 5zpf: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 288 K (3)

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 288 K (3)

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 288 K (3):
1.4.3.21;

Protein crystallography data

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 288 K (3), PDB code: 5zpf 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) 47.67 / 1.76
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 193.379, 64.225, 158.773, 90.00, 117.08, 90.00
R / Rfree (%) 15.5 / 17.9

Other elements in 5zpf:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 288 K (3) also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 288 K (3) (pdb code 5zpf). 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 6 at 288 K (3), PDB code: 5zpf:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5zpf

Go back to Copper Binding Sites List in 5zpf
Copper binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 288 K (3)


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 6 at 288 K (3) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1001

b:16.4
occ:1.00
 NE2 A:HIS431 2.0 12.8 1.0
O A:HOH1260 2.1 25.2 1.0
ND1 A:HIS592 2.1 14.6 1.0
NE2 A:HIS433 2.1 13.4 1.0
O A:HOH1429 2.2 13.1 0.6
OH A:TYQ382 2.8 18.3 0.6
CE1 A:HIS431 3.0 15.4 1.0
CD2 A:HIS431 3.0 11.1 1.0
CD2 A:HIS433 3.0 13.1 1.0
CE1 A:HIS592 3.0 16.0 1.0
CG A:HIS592 3.1 15.6 1.0
CE1 A:HIS433 3.1 15.0 1.0
CB A:HIS592 3.4 12.1 1.0
CZ A:TYQ382 3.5 24.4 0.6
O A:HOH1486 4.0 24.1 0.6
ND1 A:HIS431 4.1 11.6 1.0
CG A:HIS431 4.1 11.4 1.0
CE1 A:TYQ382 4.1 32.9 0.6
NE2 A:HIS592 4.2 14.6 1.0
CG A:HIS433 4.2 10.9 1.0
CD2 A:HIS592 4.2 10.4 1.0
ND1 A:HIS433 4.2 12.0 1.0
CE2 A:TYQ382 4.3 33.7 0.6
OZ A:TYQ382 4.3 30.3 0.4
O A:HOH1102 4.3 16.7 1.0
N5 A:TYQ382 4.4 38.0 0.6
CE A:MET602 4.6 11.6 1.0
CA A:HIS592 4.9 10.2 1.0

Copper binding site 2 out of 2 in 5zpf

Go back to Copper Binding Sites List in 5zpf
Copper binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 288 K (3)


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 6 at 288 K (3) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu701

b:15.6
occ:1.00
 NE2 B:HIS431 2.0 11.6 1.0
ND1 B:HIS592 2.0 12.8 1.0
NE2 B:HIS433 2.1 12.3 1.0
O B:HOH1018 2.1 25.6 1.0
O B:HOH1165 2.3 16.6 0.4
OH B:TYQ382 2.6 22.5 0.7
CD2 B:HIS431 2.9 9.7 1.0
CE1 B:HIS592 3.0 16.8 1.0
CE1 B:HIS431 3.0 10.1 1.0
CD2 B:HIS433 3.0 10.9 1.0
CG B:HIS592 3.0 16.5 1.0
CE1 B:HIS433 3.1 15.2 1.0
CB B:HIS592 3.4 10.9 1.0
CZ B:TYQ382 3.4 24.4 0.7
O B:HOH1239 3.8 18.0 0.5
N5 B:TYQ382 4.0 34.1 0.7
CE2 B:TYQ382 4.0 27.5 0.7
ND1 B:HIS431 4.1 12.4 1.0
CG B:HIS431 4.1 9.9 1.0
NE2 B:HIS592 4.1 13.5 1.0
CD2 B:HIS592 4.2 16.1 1.0
CE1 B:TYQ382 4.2 25.4 0.7
CG B:HIS433 4.2 11.7 1.0
ND1 B:HIS433 4.2 12.3 1.0
O B:HOH816 4.3 12.9 1.0
OZ B:TYQ382 4.6 25.9 0.3
CE B:MET602 4.6 24.5 0.2
SD B:MET602 4.9 22.6 0.8
CA B:HIS592 4.9 10.1 1.0

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 05:50:22 2025

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