Atomistry » Potassium » PDB 3vuw-3zns » 3x3y
Atomistry »
  Potassium »
    PDB 3vuw-3zns »
      3x3y »

Potassium in PDB 3x3y: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Histamine

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Histamine

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Histamine:
1.4.3.21;

Protein crystallography data

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Histamine, PDB code: 3x3y 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) 36.46 / 1.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 193.471, 63.247, 157.906, 90.00, 117.73, 90.00
R / Rfree (%) 16.2 / 17.7

Other elements in 3x3y:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Histamine also contains other interesting chemical elements:

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

Potassium Binding Sites:

The binding sites of Potassium atom in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Histamine (pdb code 3x3y). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Histamine, PDB code: 3x3y:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 3x3y

Go back to Potassium Binding Sites List in 3x3y
Potassium binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Histamine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Histamine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K710

b:16.0
occ:1.00
O A:VAL79 2.6 14.4 0.6
O A:VAL79 2.6 14.4 0.4
O A:THR80 2.8 16.1 1.0
C A:THR80 3.5 18.0 1.0
C A:VAL79 3.8 13.8 0.6
C A:VAL79 3.8 13.8 0.4
N A:GLY82 3.8 15.2 1.0
CA A:THR80 4.1 16.4 1.0
CA A:GLY82 4.2 15.2 1.0
N A:ASN81 4.2 15.2 1.0
C A:ASN81 4.3 17.3 1.0
O A:HOH979 4.4 19.7 1.0
OE1 A:GLU22 4.4 17.7 1.0
N A:THR80 4.4 13.9 1.0
CA A:ASN81 4.6 17.0 1.0
CG A:GLU22 4.7 14.7 1.0
CA A:VAL79 4.9 13.0 0.6
CD A:GLU22 5.0 18.4 1.0
CA A:VAL79 5.0 13.0 0.4

Potassium binding site 2 out of 2 in 3x3y

Go back to Potassium Binding Sites List in 3x3y
Potassium binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Histamine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Histamine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K707

b:38.9
occ:1.00
O B:HOH1341 2.6 36.4 1.0
O B:VAL79 2.7 31.9 1.0
O B:HOH1321 2.8 45.6 1.0
O B:THR80 3.0 40.3 1.0
C B:THR80 3.6 36.4 1.0
C B:VAL79 3.9 30.2 1.0
CA B:THR80 4.2 35.8 1.0
O B:HOH1230 4.2 40.2 1.0
OE2 B:GLU22 4.2 35.1 1.0
N B:ASN81 4.5 35.1 0.6
N B:ASN81 4.5 35.2 0.4
N B:THR80 4.5 30.3 1.0
N B:GLY82 4.5 32.8 1.0
C B:ASN81 4.8 35.0 0.4
CA B:ASN81 4.8 35.5 0.4
C B:ASN81 4.8 34.9 0.6
CG B:GLU22 4.9 31.2 1.0
CD B:GLU22 4.9 31.6 1.0
CA B:ASN81 4.9 35.4 0.6

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 Dec 13 23:25:19 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy