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Copper in PDB 2cwv: Product Schiff-Base Intermediate of Copper Amine Oxidase From Arthrobacter Globiformis

Enzymatic activity of Product Schiff-Base Intermediate of Copper Amine Oxidase From Arthrobacter Globiformis

All present enzymatic activity of Product Schiff-Base Intermediate of Copper Amine Oxidase From Arthrobacter Globiformis:
1.4.3.6;

Protein crystallography data

The structure of Product Schiff-Base Intermediate of Copper Amine Oxidase From Arthrobacter Globiformis, PDB code: 2cwv was solved by Y.C.Chiu, T.Okajima, T.Murakawa, M.Uchida, M.Taki, S.Hirota, M.Kim, H.Yamaguchi, Y.Kawano, N.Kamiya, S.Kuroda, H.Hayashi, Y.Yamamoto, K.Tanizawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 1.85
Space group I 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 157.702, 62.849, 184.125, 90.00, 112.43, 90.00
R / Rfree (%) 20.1 / 23.1

Copper Binding Sites:

The binding sites of Copper atom in the Product Schiff-Base Intermediate of Copper Amine Oxidase From Arthrobacter Globiformis (pdb code 2cwv). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Product Schiff-Base Intermediate of Copper Amine Oxidase From Arthrobacter Globiformis, PDB code: 2cwv:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 2cwv

Go back to Copper Binding Sites List in 2cwv
Copper binding site 1 out of 2 in the Product Schiff-Base Intermediate of Copper Amine Oxidase From Arthrobacter Globiformis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Product Schiff-Base Intermediate of Copper Amine Oxidase From Arthrobacter Globiformis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1001

b:17.2
occ:1.00
NE2 A:HIS431 2.1 14.2 1.0
NE2 A:HIS433 2.1 12.4 1.0
ND1 A:HIS592 2.2 18.7 1.0
O A:HOH1342 2.3 26.3 1.0
O A:HOH1119 2.4 35.4 1.0
CD2 A:HIS433 2.9 12.1 1.0
CE1 A:HIS431 3.1 14.4 1.0
CD2 A:HIS431 3.1 12.8 1.0
CG A:HIS592 3.1 18.0 1.0
CE1 A:HIS592 3.2 18.0 1.0
CE1 A:HIS433 3.2 14.2 1.0
CB A:HIS592 3.3 13.6 1.0
O A:HOH1281 3.7 33.9 1.0
CG A:HIS433 4.1 14.2 1.0
ND1 A:HIS431 4.2 12.1 1.0
CG A:HIS431 4.2 13.4 1.0
O A:HOH1121 4.2 24.7 1.0
ND1 A:HIS433 4.3 13.2 1.0
CD2 A:HIS592 4.3 17.9 1.0
NE2 A:HIS592 4.3 18.6 1.0
O A:HOH1074 4.3 22.0 1.0
OX1 A:2TY382 4.6 33.3 1.0
CA A:HIS592 4.9 13.1 1.0
SD A:MET602 4.9 30.1 1.0

Copper binding site 2 out of 2 in 2cwv

Go back to Copper Binding Sites List in 2cwv
Copper binding site 2 out of 2 in the Product Schiff-Base Intermediate of Copper Amine Oxidase From Arthrobacter Globiformis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Product Schiff-Base Intermediate of Copper Amine Oxidase From Arthrobacter Globiformis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1002

b:19.8
occ:1.00
NE2 B:HIS431 2.1 16.0 1.0
NE2 B:HIS433 2.2 15.4 1.0
ND1 B:HIS592 2.2 18.8 1.0
O B:HOH1289 2.6 36.4 1.0
CD2 B:HIS433 2.9 16.0 1.0
CD2 B:HIS431 3.1 14.8 1.0
CE1 B:HIS431 3.1 14.4 1.0
CG B:HIS592 3.1 19.8 1.0
CE1 B:HIS592 3.2 19.9 1.0
CE1 B:HIS433 3.3 16.2 1.0
CB B:HIS592 3.3 15.6 1.0
CG B:HIS433 4.2 15.6 1.0
ND1 B:HIS431 4.2 14.5 1.0
CG B:HIS431 4.2 15.0 1.0
CD2 B:HIS592 4.3 20.7 1.0
NE2 B:HIS592 4.3 20.0 1.0
ND1 B:HIS433 4.3 14.9 1.0
O B:HOH1157 4.4 20.4 1.0
O B:HOH1303 4.6 30.0 1.0
OX1 B:2TY382 4.7 31.3 1.0
O B:HOH1533 4.8 43.8 1.0
SD B:MET602 4.8 31.6 1.0
CA B:HIS592 4.9 14.6 1.0
CE B:MET602 5.0 32.7 1.0

Reference:

Y.C.Chiu, T.Okajima, T.Murakawa, M.Uchida, M.Taki, S.Hirota, M.Kim, H.Yamaguchi, Y.Kawano, N.Kamiya, S.Kuroda, H.Hayashi, Y.Yamamoto, K.Tanizawa. Kinetic and Structural Studies on the Catalytic Role of the Aspartic Acid Residue Conserved in Copper Amine Oxidase(,) Biochemistry V. 45 4105 2006.
ISSN: ISSN 0006-2960
PubMed: 16566584
DOI: 10.1021/BI052464L
Page generated: Thu Sep 3 16:34:17 2020
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