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Copper in PDB 2e2u: Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with 4-Hydroxybenzylhydrazine

Enzymatic activity of Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with 4-Hydroxybenzylhydrazine

All present enzymatic activity of Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with 4-Hydroxybenzylhydrazine:
1.4.3.6;

Protein crystallography data

The structure of Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with 4-Hydroxybenzylhydrazine, PDB code: 2e2u was solved by T.Murakawa, T.Okajima, M.Taki, Y.Yamamoto, H.Hayashi, K.Tanizawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.57 / 1.68
Space group I 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 157.967, 63.070, 184.052, 90.00, 112.04, 90.00
R / Rfree (%) 20.9 / 23.6

Copper Binding Sites:

The binding sites of Copper atom in the Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with 4-Hydroxybenzylhydrazine (pdb code 2e2u). 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 4-Hydroxybenzylhydrazine, PDB code: 2e2u:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 2e2u

Go back to Copper Binding Sites List in 2e2u
Copper binding site 1 out of 2 in the Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with 4-Hydroxybenzylhydrazine


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 4-Hydroxybenzylhydrazine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:25.0
occ:1.00
NE2 A:HIS431 2.1 22.6 1.0
NE2 A:HIS433 2.1 20.9 1.0
ND1 A:HIS592 2.2 26.9 1.0
O A:HOH1203 2.5 35.5 1.0
CD2 A:HIS433 3.0 22.4 1.0
CD2 A:HIS431 3.0 21.6 1.0
CG A:HIS592 3.1 23.7 1.0
CE1 A:HIS431 3.1 22.8 1.0
CE1 A:HIS592 3.2 25.6 1.0
CE1 A:HIS433 3.2 20.7 1.0
CB A:HIS592 3.4 21.5 1.0
CG A:HIS433 4.2 20.3 1.0
CG A:HIS431 4.2 21.2 1.0
ND1 A:HIS431 4.2 21.6 1.0
ND1 A:HIS433 4.3 19.9 1.0
NE2 A:HIS592 4.3 23.9 1.0
CD2 A:HIS592 4.3 24.1 1.0
O A:HOH1222 4.3 29.6 1.0
O A:HOH1136 4.4 23.8 1.0
OX1 A:4HL382 4.6 32.0 1.0
SD A:MET602 4.9 33.8 1.0
CA A:HIS592 4.9 20.3 1.0

Copper binding site 2 out of 2 in 2e2u

Go back to Copper Binding Sites List in 2e2u
Copper binding site 2 out of 2 in the Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with 4-Hydroxybenzylhydrazine


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 4-Hydroxybenzylhydrazine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu701

b:23.1
occ:1.00
NE2 B:HIS431 2.1 20.9 1.0
NE2 B:HIS433 2.1 17.5 1.0
ND1 B:HIS592 2.2 24.3 1.0
O B:HOH1465 2.7 36.7 1.0
CD2 B:HIS433 2.9 21.1 1.0
CD2 B:HIS431 3.0 19.1 1.0
CE1 B:HIS431 3.1 19.9 1.0
CG B:HIS592 3.1 21.5 1.0
CE1 B:HIS433 3.2 19.5 1.0
CE1 B:HIS592 3.2 24.2 1.0
CB B:HIS592 3.4 20.6 1.0
O B:HOH1206 3.7 46.1 1.0
CG B:HIS433 4.1 17.6 1.0
ND1 B:HIS431 4.2 19.9 1.0
CG B:HIS431 4.2 18.5 1.0
ND1 B:HIS433 4.2 17.9 1.0
NE2 B:HIS592 4.3 23.5 1.0
CD2 B:HIS592 4.3 23.8 1.0
O B:HOH874 4.4 23.4 1.0
O B:HOH945 4.6 28.3 1.0
OX1 B:4HL382 4.6 33.3 1.0
SD B:MET602 4.9 33.7 1.0
CA B:HIS592 4.9 20.2 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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