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Copper in PDB 5zpj: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 6 at 288 K (1)

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 6 at 288 K (1)

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 6 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 6 at 288 K (1), PDB code: 5zpj 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) 35.43 / 1.65
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 192.960, 64.597, 158.901, 90.00, 116.89, 90.00
R / Rfree (%) 15.4 / 17.5

Other elements in 5zpj:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 6 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 6 at 288 K (1) (pdb code 5zpj). 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 6 at 288 K (1), PDB code: 5zpj:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5zpj

Go back to Copper Binding Sites List in 5zpj
Copper binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 6 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 6 at 288 K (1) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:12.2
occ:1.00
NE2 A:HIS431 2.0 8.9 1.0
ND1 A:HIS592 2.0 13.0 1.0
NE2 A:HIS433 2.1 10.4 1.0
O A:HOH1102 2.1 19.6 1.0
O A:HOH1229 2.5 12.7 1.0
CE1 A:HIS431 3.0 11.9 1.0
CE1 A:HIS592 3.0 15.9 1.0
CD2 A:HIS431 3.0 8.4 1.0
CD2 A:HIS433 3.0 9.3 1.0
CE1 A:HIS433 3.1 14.0 1.0
CG A:HIS592 3.1 12.9 1.0
CB A:HIS592 3.4 9.2 1.0
O A:HOH1238 3.9 53.1 1.0
O A:HOH1228 4.1 35.5 1.0
ND1 A:HIS431 4.1 8.5 1.0
NE2 A:HIS592 4.1 12.9 1.0
CG A:HIS431 4.1 8.9 1.0
ND1 A:HIS433 4.2 10.8 1.0
CG A:HIS433 4.2 8.4 1.0
CD2 A:HIS592 4.2 10.6 1.0
O A:HOH961 4.4 13.0 1.0
OX1 A:2TY382 4.8 14.1 1.0
SD A:MET602 4.9 23.5 1.0
CA A:HIS592 4.9 8.8 1.0
CE A:MET602 5.0 29.1 1.0

Copper binding site 2 out of 2 in 5zpj

Go back to Copper Binding Sites List in 5zpj
Copper binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 6 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 6 at 288 K (1) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu701

b:11.8
occ:1.00
O B:HOH1121 2.0 18.7 1.0
NE2 B:HIS431 2.0 9.3 1.0
NE2 B:HIS433 2.0 8.5 1.0
CD2 B:HIS592 2.1 9.6 1.0
O B:HOH1251 2.5 15.8 1.0
CE1 B:HIS431 2.9 11.2 1.0
CG B:HIS592 3.0 12.0 1.0
CD2 B:HIS431 3.0 9.5 1.0
CE1 B:HIS433 3.0 12.9 1.0
CD2 B:HIS433 3.0 8.8 1.0
NE2 B:HIS592 3.2 17.6 1.0
CB B:HIS592 3.4 10.3 1.0
O B:HOH1241 4.0 31.9 1.0
ND1 B:HIS431 4.1 9.3 1.0
CG B:HIS431 4.1 7.8 1.0
ND1 B:HIS433 4.1 10.9 1.0
ND1 B:HIS592 4.2 17.8 1.0
CG B:HIS433 4.2 8.8 1.0
CE1 B:HIS592 4.2 8.2 1.0
O B:HOH981 4.3 11.1 1.0
CG2 B:VAL406 4.8 16.9 0.3
OX1 B:2TY382 4.8 15.2 1.0
SD B:MET602 4.9 22.0 1.0
CA B:HIS592 4.9 7.9 1.0
CE B:MET602 5.0 18.6 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: Wed Jul 31 05:45:15 2024

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