Atomistry » Chlorine » PDB 3x20-3zh8 » 3x3z
Atomistry »
  Chlorine »
    PDB 3x20-3zh8 »
      3x3z »

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: Sun Jul 21 07:55:37 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy