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Zinc in PDB 2wgq: Zinc Substituted E Coli Copper Amine Oxidase, A Model For the Precursor For 2,4,5-Trihydroxyphenylalaninequinone Formation

Enzymatic activity of Zinc Substituted E Coli Copper Amine Oxidase, A Model For the Precursor For 2,4,5-Trihydroxyphenylalaninequinone Formation

All present enzymatic activity of Zinc Substituted E Coli Copper Amine Oxidase, A Model For the Precursor For 2,4,5-Trihydroxyphenylalaninequinone Formation:
1.4.3.6;

Protein crystallography data

The structure of Zinc Substituted E Coli Copper Amine Oxidase, A Model For the Precursor For 2,4,5-Trihydroxyphenylalaninequinone Formation, PDB code: 2wgq was solved by P.C.E.Moody, R.A.Cooper, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.72 / 2.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 134.680, 166.210, 79.420, 90.00, 90.00, 90.00
R / Rfree (%) 20.403 / 26.398

Other elements in 2wgq:

The structure of Zinc Substituted E Coli Copper Amine Oxidase, A Model For the Precursor For 2,4,5-Trihydroxyphenylalaninequinone Formation also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Zinc Substituted E Coli Copper Amine Oxidase, A Model For the Precursor For 2,4,5-Trihydroxyphenylalaninequinone Formation (pdb code 2wgq). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Zinc Substituted E Coli Copper Amine Oxidase, A Model For the Precursor For 2,4,5-Trihydroxyphenylalaninequinone Formation, PDB code: 2wgq:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2wgq

Go back to Zinc Binding Sites List in 2wgq
Zinc binding site 1 out of 2 in the Zinc Substituted E Coli Copper Amine Oxidase, A Model For the Precursor For 2,4,5-Trihydroxyphenylalaninequinone Formation


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Zinc Substituted E Coli Copper Amine Oxidase, A Model For the Precursor For 2,4,5-Trihydroxyphenylalaninequinone Formation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn801

b:25.7
occ:1.00
 NE2 A:HIS526 2.0 21.4 1.0
ND1 A:HIS689 2.1 20.8 1.0
NE2 A:HIS524 2.1 16.6 1.0
OH A:TYR466 2.1 28.8 1.0
CZ A:TYR466 2.9 24.9 1.0
CE1 A:HIS524 2.9 13.0 1.0
CE1 A:HIS689 2.9 24.8 1.0
CE1 A:HIS526 3.0 19.9 1.0
CD2 A:HIS526 3.0 20.4 1.0
CG A:HIS689 3.1 20.7 1.0
CD2 A:HIS524 3.2 17.7 1.0
CE1 A:TYR466 3.6 26.5 1.0
CB A:HIS689 3.6 20.2 1.0
CE2 A:TYR466 3.7 25.0 1.0
O A:HOH2108 4.0 25.4 1.0
ND1 A:HIS526 4.1 20.1 1.0
CG A:HIS526 4.1 20.5 1.0
ND1 A:HIS524 4.1 15.8 1.0
NE2 A:HIS689 4.1 23.6 1.0
CD2 A:HIS689 4.2 22.4 1.0
CG A:HIS524 4.2 17.7 1.0
CD1 A:TYR466 4.8 22.3 1.0
CG A:GLU490 4.8 26.7 1.0
SD A:MET699 4.8 20.8 1.0
CD2 A:TYR466 4.9 24.4 1.0

Zinc binding site 2 out of 2 in 2wgq

Go back to Zinc Binding Sites List in 2wgq
Zinc binding site 2 out of 2 in the Zinc Substituted E Coli Copper Amine Oxidase, A Model For the Precursor For 2,4,5-Trihydroxyphenylalaninequinone Formation


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Zinc Substituted E Coli Copper Amine Oxidase, A Model For the Precursor For 2,4,5-Trihydroxyphenylalaninequinone Formation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn801

b:23.7
occ:1.00
 OH B:TYR466 1.9 16.4 1.0
NE2 B:HIS526 2.1 19.2 1.0
NE2 B:HIS524 2.1 15.8 1.0
ND1 B:HIS689 2.2 17.2 1.0
CZ B:TYR466 2.8 18.6 1.0
CE1 B:HIS526 2.9 20.2 1.0
CE1 B:HIS689 3.0 17.0 1.0
CE1 B:HIS524 3.1 18.1 1.0
CD2 B:HIS526 3.1 18.8 1.0
CD2 B:HIS524 3.2 17.3 1.0
CG B:HIS689 3.2 18.3 1.0
CE1 B:TYR466 3.3 21.4 1.0
CB B:HIS689 3.6 20.7 1.0
CE2 B:TYR466 3.9 18.1 1.0
O B:HOH2120 4.0 27.8 1.0
ND1 B:HIS526 4.0 20.1 1.0
CG B:HIS526 4.1 18.5 1.0
NE2 B:HIS689 4.2 14.8 1.0
ND1 B:HIS524 4.2 17.3 1.0
CG B:HIS524 4.3 18.3 1.0
CD2 B:HIS689 4.3 16.6 1.0
CD1 B:TYR466 4.6 20.8 1.0
SD B:MET699 4.8 19.4 1.0
CE B:MET699 4.8 12.9 1.0

Reference:

P.C.E.Moody, R.A.Cooper. The Structure of E Coli Amine Oxidase with the Cataltyic Copper Subsituted For Zinc - A Model Precursor. To Be Published.
Page generated: Thu Oct 17 04:54:00 2024

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