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Calcium 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:

Zinc (Zn) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium 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 Calcium atom.
In total 4 binding sites of Calcium 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 Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in 2wgq

Go back to Calcium Binding Sites List in 2wgq
Calcium binding site 1 out of 4 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 Calcium with other atoms in the Ca 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:Ca802

b:23.1
occ:1.00
 OD1 A:ASP535 2.1 23.6 1.0
O A:LEU534 2.3 21.6 1.0
O A:ALA679 2.4 19.6 1.0
OD1 A:ASP678 2.4 23.7 1.0
OD1 A:ASP533 2.4 25.9 1.0
O A:HOH2179 2.5 28.5 1.0
C A:LEU534 3.3 21.2 1.0
CG A:ASP535 3.4 22.5 1.0
C A:ALA679 3.5 20.7 1.0
CG A:ASP533 3.6 24.1 1.0
N A:ALA679 3.6 22.6 1.0
CG A:ASP678 3.6 26.6 1.0
NZ A:LYS133 3.7 19.3 1.0
N A:ASP535 4.0 20.6 1.0
CA A:ASP535 4.0 20.8 1.0
C A:ASP533 4.0 21.9 1.0
N A:LEU534 4.1 21.8 1.0
CA A:ALA679 4.1 21.4 1.0
OD2 A:ASP533 4.2 26.2 1.0
O A:ASP533 4.2 22.6 1.0
C A:ASP678 4.2 24.3 1.0
CA A:LEU534 4.3 21.4 1.0
OD2 A:ASP535 4.3 23.3 1.0
CB A:ASP535 4.3 21.6 1.0
OD2 A:ASP678 4.4 29.5 1.0
CA A:ASP678 4.4 25.4 1.0
CA A:ASP533 4.5 21.5 1.0
O A:GLU539 4.6 24.3 1.0
N A:VAL680 4.6 19.9 1.0
CB A:ASP533 4.6 22.3 1.0
CB A:ASP678 4.6 25.2 1.0
ND2 A:ASN541 4.7 23.6 1.0
CG2 A:VAL680 4.8 19.7 1.0
CB A:ALA679 4.9 21.1 1.0
CA A:VAL680 4.9 20.2 1.0

Calcium binding site 2 out of 4 in 2wgq

Go back to Calcium Binding Sites List in 2wgq
Calcium binding site 2 out of 4 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 Calcium with other atoms in the Ca 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
A:Ca803

b:29.7
occ:1.00
 O A:TYR667 2.2 27.6 1.0
OE1 A:GLU672 2.4 27.2 1.0
OE2 A:GLU573 2.5 32.6 1.0
OE1 A:GLU573 2.6 29.3 1.0
OD1 A:ASP670 2.7 30.5 1.0
CD A:GLU573 2.9 28.8 1.0
C A:TYR667 3.4 27.5 1.0
OD2 A:ASP670 3.4 32.7 1.0
CG A:ASP670 3.4 32.3 1.0
CD A:GLU672 3.5 29.6 1.0
CG A:GLU672 4.0 30.6 1.0
CE1 A:HIS644 4.1 32.5 1.0
CA A:TYR667 4.2 26.6 1.0
N A:SER668 4.3 28.7 1.0
OE2 A:GLU647 4.4 34.5 1.0
CG A:GLU573 4.4 30.3 1.0
CB A:GLU672 4.4 30.7 1.0
ND1 A:HIS644 4.5 30.4 1.0
CA A:SER668 4.5 30.1 1.0
OE2 A:GLU672 4.6 29.9 1.0
CB A:ARG642 4.7 26.4 1.0
N A:ARG642 4.7 24.0 1.0
CB A:TYR667 4.7 26.6 1.0
OE1 A:GLU647 4.7 34.1 1.0
O A:ARG642 4.9 25.5 1.0
O A:HOH2217 4.9 40.7 1.0
CB A:ASP670 4.9 33.3 1.0
CB A:THR641 4.9 21.6 1.0
N A:GLU672 5.0 31.8 1.0
CD A:GLU647 5.0 31.9 1.0

Calcium binding site 3 out of 4 in 2wgq

Go back to Calcium Binding Sites List in 2wgq
Calcium binding site 3 out of 4 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 Calcium with other atoms in the Ca binding site number 3 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:Ca802

b:26.7
occ:1.00
 OD1 B:ASP535 2.2 27.4 1.0
O B:ALA679 2.3 23.3 1.0
OD1 B:ASP533 2.4 20.0 1.0
OD1 B:ASP678 2.5 23.9 1.0
O B:HOH2139 2.5 22.8 1.0
O B:LEU534 2.9 22.8 1.0
C B:LEU534 3.3 21.6 1.0
CG B:ASP535 3.4 24.2 1.0
C B:ALA679 3.5 22.7 1.0
CG B:ASP533 3.6 19.3 1.0
CG B:ASP678 3.6 24.3 1.0
N B:ASP535 3.7 22.3 1.0
N B:ALA679 3.7 23.1 1.0
CA B:ASP535 3.9 22.4 1.0
C B:ASP533 3.9 19.0 1.0
N B:LEU534 3.9 19.9 1.0
NZ B:LYS133 4.0 25.1 1.0
CA B:ALA679 4.1 22.8 1.0
O B:ASP533 4.2 20.5 1.0
C B:ASP678 4.2 23.9 1.0
CB B:ASP535 4.3 21.9 1.0
CA B:LEU534 4.3 20.8 1.0
CA B:ASP533 4.3 18.0 1.0
OD2 B:ASP678 4.3 24.8 1.0
OD2 B:ASP535 4.3 24.5 1.0
OD2 B:ASP533 4.4 19.9 1.0
CA B:ASP678 4.5 24.2 1.0
ND2 B:ASN541 4.5 28.6 1.0
CB B:ASP533 4.6 17.5 1.0
O B:GLU539 4.6 30.7 1.0
N B:VAL680 4.6 21.6 1.0
CB B:ASP678 4.7 23.6 1.0
CB B:ALA679 4.9 23.2 1.0
CA B:VAL680 4.9 21.1 1.0
O B:ASP678 4.9 24.5 1.0

Calcium binding site 4 out of 4 in 2wgq

Go back to Calcium Binding Sites List in 2wgq
Calcium binding site 4 out of 4 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 Calcium with other atoms in the Ca binding site number 4 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:Ca803

b:24.5
occ:1.00
 O B:TYR667 2.2 28.8 1.0
OE2 B:GLU672 2.4 23.4 1.0
OE1 B:GLU573 2.4 31.7 1.0
OE2 B:GLU573 2.5 31.4 1.0
OD1 B:ASP670 2.6 37.6 1.0
CD B:GLU573 2.8 32.5 1.0
CD B:GLU672 3.3 28.5 1.0
OD2 B:ASP670 3.3 34.4 1.0
CG B:ASP670 3.3 35.8 1.0
C B:TYR667 3.5 29.4 1.0
CG B:GLU672 3.5 28.1 1.0
CB B:GLU672 4.3 28.7 1.0
CA B:SER668 4.3 31.4 1.0
N B:SER668 4.4 30.4 1.0
CG B:GLU573 4.4 32.6 1.0
CA B:TYR667 4.4 28.9 1.0
NE2 B:HIS644 4.4 32.9 1.0
CD2 B:HIS644 4.4 32.6 1.0
OE1 B:GLU672 4.5 32.2 1.0
OE2 B:GLU647 4.5 37.9 1.0
O B:HOH2165 4.5 14.5 1.0
OE1 B:GLU647 4.5 33.0 1.0
CB B:ARG642 4.5 27.9 1.0
N B:ARG642 4.6 26.4 1.0
N B:GLU672 4.7 29.4 1.0
CB B:ASP670 4.8 34.2 1.0
C B:SER668 4.8 32.6 1.0
CB B:TYR667 4.9 28.6 1.0
O B:ARG642 4.9 28.7 1.0
CD B:GLU647 5.0 33.6 1.0
O B:SER668 5.0 32.8 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: Fri Jul 12 18:40:56 2024

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