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Copper in PDB 5zpp: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 8 at 288 K (3)

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 8 at 288 K (3)

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 8 at 288 K (3):
1.4.3.21;

Protein crystallography data

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 8 at 288 K (3), PDB code: 5zpp 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) 40.51 / 1.81
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 193.019, 64.746, 158.925, 90.00, 117.00, 90.00
R / Rfree (%) 14.4 / 16.9

Other elements in 5zpp:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 8 at 288 K (3) 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 8 at 288 K (3) (pdb code 5zpp). 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 8 at 288 K (3), PDB code: 5zpp:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5zpp

Go back to Copper Binding Sites List in 5zpp
Copper binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 8 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 Phenylethylamine at pH 8 at 288 K (3) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu706

b:16.6
occ:1.00
NE2 A:HIS431 2.1 12.5 1.0
ND1 A:HIS592 2.1 14.8 1.0
NE2 A:HIS433 2.2 11.4 1.0
O A:HOH1178 2.3 26.3 1.0
OH A:TYQ382 2.6 13.8 0.7
CD2 A:HIS433 3.0 12.2 1.0
CG A:HIS592 3.1 14.3 1.0
CD2 A:HIS431 3.1 11.2 1.0
CE1 A:HIS431 3.1 12.8 1.0
CE1 A:HIS592 3.1 16.6 1.0
CE1 A:HIS433 3.2 14.7 1.0
CB A:HIS592 3.3 13.5 1.0
O A:HOH1229 3.4 45.4 1.0
CZ A:TYQ382 3.5 17.5 0.7
N5 A:TYQ382 4.0 30.4 0.7
CE2 A:TYQ382 4.1 22.2 0.7
CG A:HIS433 4.2 13.5 1.0
ND1 A:HIS431 4.2 12.3 1.0
CG A:HIS431 4.2 11.4 1.0
CD2 A:HIS592 4.2 15.1 1.0
NE2 A:HIS592 4.2 16.1 1.0
ND1 A:HIS433 4.3 12.8 1.0
CE1 A:TYQ382 4.3 16.8 0.7
O A:HOH892 4.4 16.2 1.0
OZ A:TYQ382 4.8 14.9 0.3
CA A:HIS592 4.9 13.4 1.0
SD A:MET602 4.9 25.3 1.0

Copper binding site 2 out of 2 in 5zpp

Go back to Copper Binding Sites List in 5zpp
Copper binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 8 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 Phenylethylamine at pH 8 at 288 K (3) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu705

b:17.1
occ:1.00
NE2 B:HIS431 2.1 13.5 1.0
NE2 B:HIS433 2.1 12.2 1.0
ND1 B:HIS592 2.2 15.9 1.0
O B:HOH1205 2.3 21.7 0.7
OH B:TYQ382 2.7 16.5 0.8
CD2 B:HIS433 3.0 14.4 1.0
CE1 B:HIS431 3.1 15.8 1.0
CD2 B:HIS431 3.1 13.5 1.0
CG B:HIS592 3.1 17.7 1.0
CE1 B:HIS592 3.2 17.6 1.0
CE1 B:HIS433 3.2 14.5 1.0
CB B:HIS592 3.3 14.1 1.0
O B:HOH1250 3.4 40.8 1.0
CZ B:TYQ382 3.5 20.3 0.8
N5 B:TYQ382 4.0 30.6 0.8
CE2 B:TYQ382 4.1 26.2 0.8
ND1 B:HIS431 4.2 12.9 1.0
CG B:HIS433 4.2 9.6 1.0
CG B:HIS431 4.2 11.2 1.0
ND1 B:HIS433 4.3 12.3 1.0
CD2 B:HIS592 4.3 14.1 1.0
NE2 B:HIS592 4.3 14.8 1.0
CE1 B:TYQ382 4.4 17.9 0.8
O B:HOH832 4.4 17.4 1.0
CA B:HIS592 4.9 13.4 1.0
OZ B:TYQ382 4.9 20.3 0.2
SD B:MET602 4.9 26.4 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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