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Copper in PDB 2cwu: Substrate Schiff-Base Intermediate of Copper Amine Oxidase From Arthrobacter Globiformis

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

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

Protein crystallography data

The structure of Substrate Schiff-Base Intermediate of Copper Amine Oxidase From Arthrobacter Globiformis, PDB code: 2cwu 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 (°) 157.840, 62.730, 183.890, 90.00, 112.31, 90.00
R / Rfree (%) 17.6 / 20.4

Copper Binding Sites:

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

Copper binding site 1 out of 2 in 2cwu

Go back to Copper Binding Sites List in 2cwu
Copper binding site 1 out of 2 in the Substrate 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 Substrate Schiff-Base Intermediate of Copper Amine Oxidase From Arthrobacter Globiformis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1001

b:14.4
occ:1.00
NE2 A:HIS431 2.1 10.4 1.0
NE2 A:HIS433 2.1 11.8 1.0
ND1 A:HIS592 2.2 16.9 1.0
O A:HOH1123 2.4 27.3 1.0
O A:HOH1357 2.4 30.6 1.0
CD2 A:HIS433 3.0 10.9 1.0
CE1 A:HIS431 3.0 11.4 1.0
CD2 A:HIS431 3.1 9.4 1.0
CG A:HIS592 3.1 15.5 1.0
CE1 A:HIS592 3.2 15.4 1.0
CE1 A:HIS433 3.3 13.0 1.0
CB A:HIS592 3.4 11.8 1.0
O A:HOH1287 3.7 32.6 1.0
ND1 A:HIS431 4.1 9.8 1.0
CG A:HIS433 4.2 10.3 1.0
CG A:HIS431 4.2 9.6 1.0
CD2 A:HIS592 4.3 17.2 1.0
ND1 A:HIS433 4.3 12.2 1.0
NE2 A:HIS592 4.3 16.7 1.0
O A:HOH1081 4.3 15.5 1.0
O A:HOH1125 4.4 23.4 1.0
OX1 A:1TY382 4.7 28.8 1.0
CA A:HIS592 4.9 11.6 1.0
SD A:MET602 4.9 27.3 1.0

Copper binding site 2 out of 2 in 2cwu

Go back to Copper Binding Sites List in 2cwu
Copper binding site 2 out of 2 in the Substrate 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 Substrate Schiff-Base Intermediate of Copper Amine Oxidase From Arthrobacter Globiformis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1002

b:15.1
occ:1.00
NE2 B:HIS431 2.1 11.5 1.0
ND1 B:HIS592 2.2 17.1 1.0
NE2 B:HIS433 2.2 11.3 1.0
O B:HOH1292 2.5 31.2 1.0
CD2 B:HIS433 2.9 13.0 1.0
CE1 B:HIS431 3.0 11.4 1.0
CG B:HIS592 3.1 17.9 1.0
CD2 B:HIS431 3.1 11.8 1.0
CE1 B:HIS592 3.2 16.6 1.0
CE1 B:HIS433 3.3 15.1 1.0
CB B:HIS592 3.3 14.1 1.0
ND1 B:HIS431 4.2 10.7 1.0
CG B:HIS433 4.2 11.8 1.0
CG B:HIS431 4.2 10.2 1.0
CD2 B:HIS592 4.2 18.7 1.0
NE2 B:HIS592 4.2 17.4 1.0
ND1 B:HIS433 4.3 11.6 1.0
O B:HOH1156 4.4 15.1 1.0
O B:HOH1306 4.7 27.0 1.0
OX1 B:1TY382 4.7 26.2 1.0
SD B:MET602 4.8 26.8 1.0
CA B:HIS592 4.9 12.8 1.0
CE B:MET602 5.0 27.9 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: Wed Oct 28 14:19:06 2020
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