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Copper in PDB 2zl8: Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Substrate Schiff-Base Intermediate Formed with Ethylamine

Enzymatic activity of Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Substrate Schiff-Base Intermediate Formed with Ethylamine

All present enzymatic activity of Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Substrate Schiff-Base Intermediate Formed with Ethylamine:
1.4.3.6;

Protein crystallography data

The structure of Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Substrate Schiff-Base Intermediate Formed with Ethylamine, PDB code: 2zl8 was solved by T.Murakawa, T.Okajima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.40 / 1.73
Space group I 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 157.759, 63.519, 184.074, 90.00, 111.90, 90.00
R / Rfree (%) 19.1 / 21.3

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Substrate Schiff-Base Intermediate Formed with Ethylamine (pdb code 2zl8). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Substrate Schiff-Base Intermediate Formed with Ethylamine, PDB code: 2zl8:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 2zl8

Go back to Copper Binding Sites List in 2zl8
Copper binding site 1 out of 2 in the Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Substrate Schiff-Base Intermediate Formed with Ethylamine


Mono view


Stereo pair view

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

b:24.7
occ:1.00
 NE2 A:HIS431 2.1 21.3 1.0
NE2 A:HIS433 2.2 19.2 1.0
O A:HOH1317 2.3 39.4 1.0
ND1 A:HIS592 2.3 34.2 1.0
CE1 A:HIS431 3.0 21.9 1.0
CD2 A:HIS433 3.0 19.2 1.0
CD2 A:HIS431 3.1 20.3 1.0
CE1 A:HIS433 3.2 20.0 1.0
CE1 A:HIS592 3.3 32.4 1.0
CG A:HIS592 3.3 31.5 1.0
CB A:HIS592 3.5 26.0 1.0
O A:HOH1081 3.7 37.6 1.0
OX A:ESB382 4.0 51.4 1.0
ND1 A:HIS431 4.2 22.0 1.0
CG A:HIS431 4.2 20.9 1.0
O A:HOH1103 4.2 25.8 1.0
CG A:HIS433 4.2 19.5 1.0
ND1 A:HIS433 4.3 17.7 1.0
CE A:MET602 4.3 38.9 1.0
NE2 A:HIS592 4.4 32.0 1.0
CD2 A:HIS592 4.4 31.9 1.0
O A:HOH1213 4.5 43.9 1.0
CD1 A:ESB382 4.8 48.8 1.0
CE1 A:ESB382 5.0 52.4 1.0

Copper binding site 2 out of 2 in 2zl8

Go back to Copper Binding Sites List in 2zl8
Copper binding site 2 out of 2 in the Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Substrate Schiff-Base Intermediate Formed with Ethylamine


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Substrate Schiff-Base Intermediate Formed with Ethylamine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1001

b:25.9
occ:1.00
 NE2 B:HIS431 2.1 20.9 1.0
NE2 B:HIS433 2.1 19.4 1.0
O B:HOH1173 2.4 41.9 1.0
ND1 B:HIS592 2.4 35.9 1.0
CD2 B:HIS433 3.0 20.9 1.0
CE1 B:HIS431 3.1 20.8 1.0
CD2 B:HIS431 3.1 21.4 1.0
CE1 B:HIS433 3.2 20.8 1.0
CE1 B:HIS592 3.3 34.2 1.0
CG B:HIS592 3.3 32.5 1.0
CB B:HIS592 3.6 26.4 1.0
CG B:HIS433 4.2 18.0 1.0
ND1 B:HIS431 4.2 20.6 1.0
CG B:HIS431 4.2 21.0 1.0
OX B:ESB382 4.3 48.2 1.0
ND1 B:HIS433 4.3 19.5 1.0
O B:HOH1098 4.3 21.7 1.0
NE2 B:HIS592 4.4 35.0 1.0
CD2 B:HIS592 4.5 34.2 1.0
O B:HOH1545 4.5 45.4 1.0
SD B:MET602 4.9 34.6 1.0

Reference:

M.Taki, T.Murakawa, T.Nakamoto, M.Uchida, H.Hayashi, K.Tanizawa, Y.Yamamoto, T.Okajima. Further Insight Into the Mechanism of Stereoselective Proton Abstraction By Bacterial Copper Amine Oxidase Biochemistry V. 47 7726 2008.
ISSN: ISSN 0006-2960
PubMed: 18627131
DOI: 10.1021/BI800623F
Page generated: Mon Jul 14 01:45:58 2025

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