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Copper in PDB 5zpm: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 7 at 288 K (2)

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 7 at 288 K (2)

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 7 at 288 K (2):
1.4.3.21;

Protein crystallography data

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 7 at 288 K (2), PDB code: 5zpm 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) 36.68 / 1.65
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 192.866, 64.320, 158.903, 90.00, 116.92, 90.00
R / Rfree (%) 14.9 / 17.1

Other elements in 5zpm:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 7 at 288 K (2) 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 Phenylethylamine at pH 7 at 288 K (2) (pdb code 5zpm). 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 Phenylethylamine at pH 7 at 288 K (2), PDB code: 5zpm:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5zpm

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


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 Phenylethylamine at pH 7 at 288 K (2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu704

b:15.8
occ:1.00
O A:HOH990 1.9 24.6 1.0
CE1 A:HIS431 2.0 11.2 1.0
NE2 A:HIS433 2.0 12.0 1.0
ND1 A:HIS592 2.0 14.7 1.0
O A:HOH1263 2.5 21.0 1.0
NE2 A:HIS431 2.8 19.9 1.0
CE1 A:HIS592 3.0 18.2 1.0
CD2 A:HIS433 3.0 14.1 1.0
CE1 A:HIS433 3.0 16.9 1.0
CG A:HIS592 3.0 15.4 1.0
ND1 A:HIS431 3.1 16.4 1.0
CB A:HIS592 3.4 13.9 1.0
CD2 A:HIS431 4.0 10.8 1.0
O A:HOH1265 4.1 30.2 0.8
NE2 A:HIS592 4.1 16.8 1.0
ND1 A:HIS433 4.1 14.7 1.0
CG A:HIS433 4.1 12.0 1.0
CG A:HIS431 4.1 12.6 1.0
CD2 A:HIS592 4.2 15.7 1.0
O A:HOH983 4.3 15.6 1.0
CE A:MET602 4.6 23.1 0.4
OX1 A:2TY382 4.8 17.6 0.5
OX1 A:2TY382 4.9 22.3 0.5
CA A:HIS592 4.9 12.5 1.0
SD A:MET602 4.9 20.7 0.6
CE A:MET602 5.0 18.0 0.6

Copper binding site 2 out of 2 in 5zpm

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


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 Phenylethylamine at pH 7 at 288 K (2) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu704

b:15.3
occ:1.00
CE1 B:HIS431 2.0 11.1 1.0
O B:HOH1118 2.0 22.7 1.0
NE2 B:HIS433 2.0 12.4 1.0
ND1 B:HIS592 2.0 15.0 1.0
O B:HOH1266 2.6 22.8 1.0
NE2 B:HIS431 2.8 18.3 1.0
CE1 B:HIS592 3.0 17.2 1.0
CD2 B:HIS433 3.0 14.0 1.0
CE1 B:HIS433 3.0 15.7 1.0
ND1 B:HIS431 3.0 16.7 1.0
CG B:HIS592 3.1 16.0 1.0
CB B:HIS592 3.4 13.1 1.0
O B:HOH1277 4.0 28.4 0.7
CD2 B:HIS431 4.1 11.6 1.0
ND1 B:HIS433 4.1 13.3 1.0
NE2 B:HIS592 4.1 13.9 1.0
CG B:HIS433 4.1 10.1 1.0
CG B:HIS431 4.2 12.2 1.0
CD2 B:HIS592 4.2 15.4 1.0
O B:HOH1059 4.3 14.5 1.0
OX1 B:2TY382 4.8 12.8 0.5
SD B:MET602 4.9 26.6 1.0
CA B:HIS592 4.9 10.8 1.0
OX1 B:2TY382 5.0 23.9 0.6

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 05:51:19 2025

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