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Copper in PDB 5zps: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 10 at 288 K (1)

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 10 at 288 K (1)

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 10 at 288 K (1):
1.4.3.21;

Protein crystallography data

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 10 at 288 K (1), PDB code: 5zps 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) 40.54 / 1.75
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 193.257, 64.797, 159.095, 90.00, 117.09, 90.00
R / Rfree (%) 15.2 / 17.7

Other elements in 5zps:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 10 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 Phenylethylamine at pH 10 at 288 K (1) (pdb code 5zps). 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 10 at 288 K (1), PDB code: 5zps:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5zps

Go back to Copper Binding Sites List in 5zps
Copper binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 10 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 Phenylethylamine at pH 10 at 288 K (1) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:15.2
occ:1.00
O A:HOH879 2.0 26.7 1.0
NE2 A:HIS431 2.0 11.0 1.0
ND1 A:HIS592 2.0 12.5 1.0
NE2 A:HIS433 2.1 11.4 1.0
OH A:TYQ382 2.8 19.9 1.0
CD2 A:HIS431 3.0 9.5 1.0
CD2 A:HIS433 3.0 11.4 1.0
CG A:HIS592 3.0 14.7 1.0
CE1 A:HIS431 3.0 11.0 1.0
CE1 A:HIS592 3.0 15.9 1.0
CE1 A:HIS433 3.1 13.1 1.0
CB A:HIS592 3.3 11.0 1.0
O A:HOH1255 3.5 44.6 1.0
CZ A:TYQ382 3.6 21.8 1.0
N5 A:TYQ382 4.1 32.2 1.0
ND1 A:HIS431 4.1 9.4 1.0
CG A:HIS431 4.1 9.3 1.0
NE2 A:HIS592 4.1 17.8 1.0
CD2 A:HIS592 4.1 16.6 1.0
CG A:HIS433 4.2 11.3 1.0
ND1 A:HIS433 4.2 10.9 1.0
CE2 A:TYQ382 4.2 26.3 1.0
CE1 A:TYQ382 4.5 17.1 1.0
O A:HOH850 4.5 16.1 1.0
CA A:HIS592 4.8 11.1 1.0
SD A:MET602 5.0 22.5 1.0

Copper binding site 2 out of 2 in 5zps

Go back to Copper Binding Sites List in 5zps
Copper binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 10 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 Phenylethylamine at pH 10 at 288 K (1) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu701

b:18.3
occ:1.00
O B:HOH806 2.0 30.4 1.0
NE2 B:HIS431 2.0 12.5 1.0
NE2 B:HIS433 2.1 13.4 1.0
ND1 B:HIS592 2.1 16.6 1.0
OH B:TYQ382 2.7 24.9 1.0
CD2 B:HIS431 3.0 11.7 1.0
CD2 B:HIS433 3.0 16.1 1.0
CE1 B:HIS431 3.1 12.7 1.0
CE1 B:HIS433 3.1 16.4 1.0
CG B:HIS592 3.1 17.4 1.0
CE1 B:HIS592 3.1 18.4 1.0
CB B:HIS592 3.3 14.3 1.0
CZ B:TYQ382 3.5 19.4 1.0
O B:HOH1242 3.6 47.9 1.0
N5 B:TYQ382 3.8 38.6 1.0
CE2 B:TYQ382 4.0 27.3 1.0
CG B:HIS431 4.1 12.8 1.0
ND1 B:HIS431 4.1 12.8 1.0
ND1 B:HIS433 4.2 13.1 1.0
CG B:HIS433 4.2 13.1 1.0
NE2 B:HIS592 4.2 14.3 1.0
CD2 B:HIS592 4.2 18.0 1.0
CE1 B:TYQ382 4.4 19.9 1.0
O B:HOH821 4.4 18.5 1.0
CG2 B:VAL406 4.6 17.4 0.4
CA B:HIS592 4.9 11.8 1.0
SD B:MET602 4.9 24.2 1.0
CE B:MET602 5.0 23.1 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 05:51:52 2025

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