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Chlorine in PDB 3x3z: Copper Amine Oxidase From Arthrobacter Globiformis: Aminoresorcinol Form Produced By Anaerobic Reduction with Ethylamine Hydrochloride

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis: Aminoresorcinol Form Produced By Anaerobic Reduction with Ethylamine Hydrochloride

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis: Aminoresorcinol Form Produced By Anaerobic Reduction with Ethylamine Hydrochloride:
1.4.3.21;

Protein crystallography data

The structure of Copper Amine Oxidase From Arthrobacter Globiformis: Aminoresorcinol Form Produced By Anaerobic Reduction with Ethylamine Hydrochloride, PDB code: 3x3z was solved by T.Okajima, S.Nakanishi, T.Murakawa, M.Kataoka, H.Hayashi, A.Hamaguchi, T.Nakai, Y.Kawano, H.Yamaguchi, K.Tanizawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 22.28 / 1.51
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 192.548, 62.729, 157.647, 90.00, 117.62, 90.00
R / Rfree (%) 16.1 / 17.8

Other elements in 3x3z:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis: Aminoresorcinol Form Produced By Anaerobic Reduction with Ethylamine Hydrochloride also contains other interesting chemical elements:

Potassium (K) 2 atoms
Copper (Cu) 2 atoms
Sodium (Na) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Copper Amine Oxidase From Arthrobacter Globiformis: Aminoresorcinol Form Produced By Anaerobic Reduction with Ethylamine Hydrochloride (pdb code 3x3z). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Copper Amine Oxidase From Arthrobacter Globiformis: Aminoresorcinol Form Produced By Anaerobic Reduction with Ethylamine Hydrochloride, PDB code: 3x3z:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 3x3z

Go back to Chlorine Binding Sites List in 3x3z
Chlorine binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis: Aminoresorcinol Form Produced By Anaerobic Reduction with Ethylamine Hydrochloride


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Copper Amine Oxidase From Arthrobacter Globiformis: Aminoresorcinol Form Produced By Anaerobic Reduction with Ethylamine Hydrochloride within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1002

b:14.7
occ:1.00
CU A:CU1001 2.5 11.9 1.0
O A:HOH1110 3.0 12.2 1.0
OZ A:TYQ382 3.1 16.4 1.0
NE2 A:HIS431 3.2 9.7 1.0
O A:HOH1342 3.4 24.6 1.0
NE2 A:HIS433 3.5 9.0 1.0
ND1 A:HIS592 3.6 11.8 1.0
CE1 A:HIS431 3.6 10.6 1.0
CE A:MET602 3.7 10.3 0.5
CE1 A:HIS433 3.7 10.3 1.0
CE1 A:HIS592 3.8 14.4 1.0
CE1 A:TYQ382 3.8 16.4 1.0
CD1 A:TYQ382 3.9 17.2 1.0
O A:HOH1160 4.0 16.0 1.0
CA A:VAL406 4.1 12.0 0.8
CG1 A:VAL406 4.2 16.3 0.8
CA A:VAL406 4.2 13.1 0.2
CD2 A:HIS431 4.2 9.5 1.0
SD A:MET602 4.3 17.4 0.5
CG2 A:VAL406 4.3 15.4 0.2
CB A:VAL406 4.4 15.3 0.8
SD A:MET602 4.4 23.4 0.5
N A:PHE407 4.6 12.1 1.0
CB A:VAL406 4.6 14.2 0.2
CG1 A:VAL406 4.6 15.9 0.2
OH A:TYR284 4.7 13.4 1.0
ND2 A:ASN381 4.7 14.4 1.0
ND1 A:HIS431 4.8 10.2 1.0
O A:VAL405 4.8 13.3 1.0
CD2 A:HIS433 4.9 11.8 1.0
CG A:HIS592 4.9 10.5 1.0
C A:VAL406 4.9 12.4 0.8
CE A:MET602 4.9 14.2 0.5
N A:VAL406 4.9 13.1 0.8
C A:VAL406 5.0 12.7 0.2
N A:VAL406 5.0 13.0 0.2
ND1 A:HIS433 5.0 10.6 1.0

Chlorine binding site 2 out of 2 in 3x3z

Go back to Chlorine Binding Sites List in 3x3z
Chlorine binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis: Aminoresorcinol Form Produced By Anaerobic Reduction with Ethylamine Hydrochloride


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Copper Amine Oxidase From Arthrobacter Globiformis: Aminoresorcinol Form Produced By Anaerobic Reduction with Ethylamine Hydrochloride within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1002

b:57.2
occ:0.39
OH B:TYQ382 0.7 7.6 0.6
CU B:CU1001 1.9 11.3 1.0
CZ B:TYQ382 2.0 18.3 0.6
NE2 B:HIS431 2.6 7.7 1.0
CE2 B:TYQ382 2.9 20.5 0.6
ND1 B:HIS592 2.9 11.7 1.0
O B:HOH1888 3.0 29.6 1.0
N5 B:TYQ382 3.0 24.4 0.6
CE1 B:TYQ382 3.0 16.3 0.6
O B:HOH1132 3.1 11.8 1.0
CE1 B:HIS431 3.1 7.7 1.0
CE1 B:HIS592 3.2 13.6 1.0
NE2 B:HIS433 3.3 8.2 1.0
CE1 B:HIS433 3.7 10.2 1.0
OZ B:TYQ382 3.8 9.8 0.4
CD2 B:HIS431 3.8 8.3 1.0
CG1 B:VAL406 3.9 17.1 0.7
CG2 B:VAL406 4.0 15.6 0.3
O B:HOH1896 4.0 31.7 1.0
CD2 B:TYQ382 4.2 19.1 0.6
CG B:HIS592 4.2 9.6 1.0
CD1 B:TYQ382 4.3 17.1 0.6
ND1 B:HIS431 4.3 9.2 1.0
CB B:VAL406 4.3 14.0 0.7
CA B:VAL406 4.4 9.5 0.7
NE2 B:HIS592 4.5 11.9 1.0
CA B:VAL406 4.5 10.4 0.3
CE1 B:TYQ382 4.6 12.3 0.4
CD2 B:HIS433 4.6 10.1 1.0
CB B:VAL406 4.6 12.9 0.3
SD B:MET602 4.6 28.5 1.0
CG B:HIS431 4.6 7.3 1.0
CG1 B:VAL406 4.7 13.2 0.3
CD1 B:TYQ382 4.7 13.9 0.4
CG B:TYQ382 4.7 13.5 0.6
OH B:TYR284 4.8 14.1 1.0
O B:HOH1140 4.8 12.2 1.0
CB B:HIS592 4.9 11.2 1.0
O B:HOH1725 4.9 36.2 1.0
CD2 B:HIS592 5.0 10.2 1.0

Reference:

T.Murakawa, A.Hamaguchi, S.Nakanishi, M.Kataoka, T.Nakai, Y.Kawano, H.Yamaguchi, H.Hayashi, K.Tanizawa, T.Okajima. Probing the Catalytic Mechanism of Copper Amine Oxidase From Arthrobacter Globiformis with Halide Ions J.Biol.Chem. 2015.
ISSN: ESSN 1083-351X
DOI: 10.1074/JBC.M115.662726
Page generated: Sat Dec 12 10:20:27 2020

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