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Copper in PDB 5zpb: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 283 K (3)

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 283 K (3)

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 283 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 283 K (3), PDB code: 5zpb 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) 37.51 / 1.79
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 193.510, 64.077, 158.651, 90.00, 117.21, 90.00
R / Rfree (%) 16.5 / 19

Other elements in 5zpb:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 283 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 283 K (3) (pdb code 5zpb). 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 283 K (3), PDB code: 5zpb:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5zpb

Go back to Copper Binding Sites List in 5zpb
Copper binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 283 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 283 K (3) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1001

b:16.6
occ:1.00
O A:HOH1254 1.9 12.7 0.5
O A:HOH1188 2.0 30.2 0.9
NE2 A:HIS431 2.0 13.3 1.0
ND1 A:HIS592 2.0 19.4 1.0
NE2 A:HIS433 2.1 12.8 1.0
OH A:TYQ382 2.7 24.5 0.7
CE1 A:HIS592 2.9 20.7 1.0
CE1 A:HIS431 3.0 17.1 1.0
CD2 A:HIS431 3.0 12.6 1.0
CE1 A:HIS433 3.1 16.3 1.0
CD2 A:HIS433 3.1 14.6 1.0
CG A:HIS592 3.1 20.2 1.0
CB A:HIS592 3.4 13.2 1.0
O A:HOH1472 3.6 50.4 1.0
CZ A:TYQ382 3.6 29.2 0.7
ND1 A:HIS431 4.1 13.1 1.0
NE2 A:HIS592 4.1 16.7 1.0
CG A:HIS431 4.1 13.2 1.0
CD2 A:HIS592 4.2 13.6 1.0
ND1 A:HIS433 4.2 12.9 1.0
CG A:HIS433 4.2 14.1 1.0
N5 A:TYQ382 4.2 42.0 0.7
CE2 A:TYQ382 4.2 37.8 0.7
OZ A:TYQ382 4.2 34.0 0.3
O A:HOH1108 4.3 16.3 1.0
CE1 A:TYQ382 4.3 35.2 0.7
CE A:MET602 4.5 25.4 1.0
CA A:HIS592 5.0 11.9 1.0

Copper binding site 2 out of 2 in 5zpb

Go back to Copper Binding Sites List in 5zpb
Copper binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 283 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 283 K (3) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu701

b:15.2
occ:1.00
NE2 B:HIS431 2.0 11.4 1.0
O B:HOH864 2.0 14.9 0.6
ND1 B:HIS592 2.0 16.2 1.0
NE2 B:HIS433 2.0 11.8 1.0
OH B:TYQ382 2.4 27.1 0.7
O B:HOH1161 2.5 16.1 0.4
CE1 B:HIS431 3.0 11.9 1.0
CE1 B:HIS433 3.0 14.5 1.0
CE1 B:HIS592 3.0 19.8 1.0
CD2 B:HIS431 3.0 9.8 1.0
CG B:HIS592 3.0 17.8 1.0
CD2 B:HIS433 3.1 11.0 1.0
CB B:HIS592 3.4 13.4 1.0
CZ B:TYQ382 3.4 29.6 0.7
O B:HOH1228 3.6 46.1 1.0
N5 B:TYQ382 3.8 44.0 0.7
CE2 B:TYQ382 4.0 37.4 0.7
ND1 B:HIS431 4.1 11.3 1.0
ND1 B:HIS433 4.1 16.1 1.0
NE2 B:HIS592 4.1 15.5 1.0
CG B:HIS431 4.2 10.1 1.0
CD2 B:HIS592 4.2 17.2 1.0
CG B:HIS433 4.2 12.6 1.0
O B:HOH943 4.2 11.9 1.0
CE1 B:TYQ382 4.4 28.2 0.7
CE B:MET602 4.4 27.2 1.0
OZ B:TYQ382 4.6 29.8 0.3
CA B:HIS592 4.9 10.6 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: Sun Dec 13 11:21:30 2020

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