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Copper in PDB 6ezz: Crystal Structure of Escherichia Coli Amine Oxidase Mutant E573Q

Enzymatic activity of Crystal Structure of Escherichia Coli Amine Oxidase Mutant E573Q

All present enzymatic activity of Crystal Structure of Escherichia Coli Amine Oxidase Mutant E573Q:
1.4.3.21;

Protein crystallography data

The structure of Crystal Structure of Escherichia Coli Amine Oxidase Mutant E573Q, PDB code: 6ezz was solved by T.G.Gaule, M.A.Smith, K.M.Tych, P.Pirrat, C.H.Trinh, A.R.Pearson, P.F.Knowles, M.J.Mcpherson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 72.12 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 135.521, 167.202, 79.939, 90.00, 90.00, 90.00
R / Rfree (%) 16.6 / 19.7

Other elements in 6ezz:

The structure of Crystal Structure of Escherichia Coli Amine Oxidase Mutant E573Q also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Escherichia Coli Amine Oxidase Mutant E573Q (pdb code 6ezz). 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 Escherichia Coli Amine Oxidase Mutant E573Q, PDB code: 6ezz:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 6ezz

Go back to Copper Binding Sites List in 6ezz
Copper binding site 1 out of 2 in the Crystal Structure of Escherichia Coli Amine Oxidase Mutant E573Q


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 Escherichia Coli Amine Oxidase Mutant E573Q within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu801

b:27.1
occ:1.00
NE2 A:HIS526 2.0 23.6 1.0
ND1 A:HIS689 2.0 23.9 1.0
NE2 A:HIS524 2.0 27.1 1.0
OH A:TYR466 2.1 31.7 1.0
CE1 A:HIS689 2.9 26.0 1.0
CE1 A:HIS526 2.9 29.0 1.0
CZ A:TYR466 2.9 31.4 1.0
CE1 A:HIS524 2.9 27.3 1.0
CD2 A:HIS526 3.0 27.7 1.0
CD2 A:HIS524 3.1 25.2 1.0
CG A:HIS689 3.1 23.9 1.0
CB A:HIS689 3.5 24.2 1.0
CE2 A:TYR466 3.6 34.9 1.0
CE1 A:TYR466 3.8 36.1 1.0
NE2 A:HIS689 4.0 25.7 1.0
ND1 A:HIS526 4.0 28.9 1.0
O A:HOH1080 4.0 28.5 1.0
ND1 A:HIS524 4.1 25.8 1.0
CG A:HIS526 4.1 26.4 1.0
CD2 A:HIS689 4.2 25.2 1.0
CG A:HIS524 4.2 26.0 1.0
CD2 A:TYR466 4.8 33.1 1.0
SD A:MET699 4.8 34.0 1.0
CE A:MET699 4.9 34.8 1.0
CD1 A:TYR466 4.9 33.1 1.0
O A:HOH936 4.9 51.7 1.0

Copper binding site 2 out of 2 in 6ezz

Go back to Copper Binding Sites List in 6ezz
Copper binding site 2 out of 2 in the Crystal Structure of Escherichia Coli Amine Oxidase Mutant E573Q


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 Escherichia Coli Amine Oxidase Mutant E573Q within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu801

b:26.9
occ:1.00
NE2 B:HIS526 2.0 26.9 1.0
OH B:TYR466 2.1 38.5 1.0
NE2 B:HIS524 2.1 24.0 1.0
ND1 B:HIS689 2.1 27.9 1.0
CE1 B:HIS526 2.9 32.8 1.0
CZ B:TYR466 2.9 36.8 1.0
CE1 B:HIS524 3.0 25.4 1.0
CE1 B:HIS689 3.0 27.9 1.0
CD2 B:HIS526 3.1 33.3 1.0
CD2 B:HIS524 3.1 25.3 1.0
CG B:HIS689 3.1 26.1 1.0
CE2 B:TYR466 3.5 42.7 1.0
CB B:HIS689 3.5 24.5 1.0
CE1 B:TYR466 3.8 40.6 1.0
ND1 B:HIS526 4.0 34.8 1.0
ND1 B:HIS524 4.1 24.6 1.0
CG B:HIS526 4.1 28.9 1.0
NE2 B:HIS689 4.2 27.7 1.0
CG B:HIS524 4.2 25.2 1.0
CD2 B:HIS689 4.2 25.3 1.0
OE1 B:GLU490 4.2 62.2 1.0
O B:HOH1110 4.3 28.1 1.0
CD2 B:TYR466 4.7 38.8 1.0
CE B:MET699 4.8 38.0 1.0
SD B:MET699 4.8 37.1 1.0
CD1 B:TYR466 5.0 36.2 1.0

Reference:

T.G.Gaule, M.A.Smith, K.M.Tych, P.Pirrat, C.H.Trinh, A.R.Pearson, P.F.Knowles, M.J.Mcpherson. Oxygen Activation Switch in the Copper Amine Oxidase of Escherichia Coli. Biochemistry V. 57 5301 2018.
ISSN: ISSN 1520-4995
PubMed: 30110143
DOI: 10.1021/ACS.BIOCHEM.8B00633
Page generated: Sun Dec 13 11:22:16 2020

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