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Copper in PDB 2e2v: Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Benzylhydrazine

Enzymatic activity of Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Benzylhydrazine

All present enzymatic activity of Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Benzylhydrazine:
1.4.3.6;

Protein crystallography data

The structure of Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Benzylhydrazine, PDB code: 2e2v was solved by T.Murakawa, T.Okajima, M.Taki, Y.Yamamoto, S.Kuroda, H.Hayashi, K.Tanizawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.52 / 1.80
Space group I 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 158.054, 62.640, 183.951, 90.00, 112.16, 90.00
R / Rfree (%) 21.7 / 25.2

Copper Binding Sites:

The binding sites of Copper atom in the Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Benzylhydrazine (pdb code 2e2v). 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 Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Benzylhydrazine, PDB code: 2e2v:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 2e2v

Go back to Copper Binding Sites List in 2e2v
Copper binding site 1 out of 2 in the Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Benzylhydrazine


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 Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Benzylhydrazine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:26.9
occ:1.00
NE2 A:HIS431 2.1 21.9 1.0
ND1 A:HIS592 2.1 27.6 1.0
NE2 A:HIS433 2.2 21.9 1.0
O A:HOH1649 2.5 38.4 1.0
O A:HOH1353 2.5 47.9 1.0
CD2 A:HIS433 3.0 22.4 1.0
CD2 A:HIS431 3.1 21.1 1.0
CG A:HIS592 3.1 25.7 1.0
CE1 A:HIS431 3.1 22.5 1.0
CE1 A:HIS592 3.1 27.2 1.0
CE1 A:HIS433 3.3 22.0 1.0
CB A:HIS592 3.3 22.4 1.0
O A:HOH1590 3.7 53.8 1.0
CG A:HIS433 4.2 21.4 1.0
CG A:HIS431 4.2 22.1 1.0
ND1 A:HIS431 4.2 22.3 1.0
NE2 A:HIS592 4.2 25.7 1.0
CD2 A:HIS592 4.2 26.9 1.0
ND1 A:HIS433 4.3 20.6 1.0
O A:HOH1254 4.4 30.6 1.0
O A:HOH1132 4.4 24.6 1.0
O2 A:3TY382 4.6 36.4 1.0
CA A:HIS592 4.9 21.5 1.0
SD A:MET602 4.9 34.5 1.0
CE A:MET602 5.0 32.7 1.0

Copper binding site 2 out of 2 in 2e2v

Go back to Copper Binding Sites List in 2e2v
Copper binding site 2 out of 2 in the Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Benzylhydrazine


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 Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Benzylhydrazine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu701

b:22.7
occ:1.00
NE2 B:HIS431 2.1 22.7 1.0
NE2 B:HIS433 2.1 17.8 1.0
ND1 B:HIS592 2.1 22.8 1.0
O B:HOH953 2.7 34.7 1.0
CD2 B:HIS433 2.9 20.1 1.0
CE1 B:HIS431 3.0 21.3 1.0
CG B:HIS592 3.1 23.5 1.0
CD2 B:HIS431 3.1 19.8 1.0
CE1 B:HIS592 3.1 24.7 1.0
CE1 B:HIS433 3.2 20.5 1.0
CB B:HIS592 3.3 20.3 1.0
CG B:HIS433 4.1 16.8 1.0
ND1 B:HIS431 4.1 22.2 1.0
CG B:HIS431 4.2 19.8 1.0
ND1 B:HIS433 4.2 16.8 1.0
NE2 B:HIS592 4.2 23.5 1.0
CD2 B:HIS592 4.2 24.6 1.0
O B:HOH906 4.4 21.3 1.0
O2 B:3TY382 4.6 29.5 1.0
O B:HOH1006 4.6 28.1 1.0
CA B:HIS592 4.9 19.3 1.0
SD B:MET602 4.9 31.7 1.0

Reference:

T.Murakawa, T.Okajima, M.Taki, Y.Yamamoto, S.Kuroda, H.Hayashi, K.Tanizawa. Catalytic Regulation Conducted By the Substrate Schiff Base and Conserved Aspartic Acid Residue in Bacterial Copper Amine Oxidase Reaction To Be Published.
Page generated: Thu Sep 3 16:35:37 2020
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