Atomistry » Copper » PDB 1hc1-1jvo » 1iu7
Atomistry »
  Copper »
    PDB 1hc1-1jvo »
      1iu7 »

Copper in PDB 1iu7: Holo Form of Copper-Containing Amine Oxidase From Arthrobacter Globiformis

Enzymatic activity of Holo Form of Copper-Containing Amine Oxidase From Arthrobacter Globiformis

All present enzymatic activity of Holo Form of Copper-Containing Amine Oxidase From Arthrobacter Globiformis:
1.4.3.6;

Protein crystallography data

The structure of Holo Form of Copper-Containing Amine Oxidase From Arthrobacter Globiformis, PDB code: 1iu7 was solved by S.Kishishita, T.Okajima, M.Kim, H.Yamaguchi, S.Hirota, S.Suzuki, S.Kuroda, K.Tanizawa, M.Mure, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.00 / 1.80
Space group I 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 157.794, 62.633, 183.956, 90.00, 111.74, 90.00
R / Rfree (%) 20.9 / 25.2

Copper Binding Sites:

The binding sites of Copper atom in the Holo Form of Copper-Containing Amine Oxidase From Arthrobacter Globiformis (pdb code 1iu7). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Holo Form of Copper-Containing Amine Oxidase From Arthrobacter Globiformis, PDB code: 1iu7:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1iu7

Go back to Copper Binding Sites List in 1iu7
Copper binding site 1 out of 2 in the Holo Form of Copper-Containing Amine Oxidase From Arthrobacter Globiformis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Holo Form of Copper-Containing Amine Oxidase From Arthrobacter Globiformis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1001

b:14.5
occ:1.00
O A:HOH1002 2.0 18.3 1.0
NE2 A:HIS431 2.1 9.9 1.0
NE2 A:HIS433 2.2 14.1 1.0
ND1 A:HIS592 2.2 14.5 1.0
O A:HOH1003 2.7 22.1 1.0
CD2 A:HIS431 3.0 7.8 1.0
CD2 A:HIS433 3.0 13.5 1.0
CE1 A:HIS431 3.1 7.5 1.0
CG A:HIS592 3.2 13.6 1.0
CE1 A:HIS592 3.2 13.5 1.0
CE1 A:HIS433 3.2 13.1 1.0
CB A:HIS592 3.4 10.6 1.0
O A:HOH1558 3.7 50.3 1.0
CG A:HIS431 4.2 5.9 1.0
ND1 A:HIS431 4.2 7.3 1.0
O A:HOH1004 4.2 22.7 1.0
CG A:HIS433 4.2 12.5 1.0
ND1 A:HIS433 4.3 11.0 1.0
NE2 A:HIS592 4.3 11.2 1.0
CD2 A:HIS592 4.3 12.3 1.0
O A:HOH1005 4.3 12.1 1.0
O2 A:TPQ382 4.7 25.6 1.0
CE A:MET602 4.8 19.7 1.0
SD A:MET602 4.9 20.3 1.0
CA A:HIS592 4.9 11.9 1.0

Copper binding site 2 out of 2 in 1iu7

Go back to Copper Binding Sites List in 1iu7
Copper binding site 2 out of 2 in the Holo Form of Copper-Containing Amine Oxidase From Arthrobacter Globiformis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Holo Form of Copper-Containing Amine Oxidase From Arthrobacter Globiformis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1002

b:11.2
occ:1.00
O B:HOH1003 2.0 13.3 1.0
NE2 B:HIS431 2.1 9.5 1.0
NE2 B:HIS433 2.2 11.9 1.0
ND1 B:HIS592 2.2 12.3 1.0
O B:HOH1004 2.8 23.7 1.0
CD2 B:HIS433 3.0 11.7 1.0
CD2 B:HIS431 3.1 5.7 1.0
CE1 B:HIS431 3.1 5.3 1.0
CG B:HIS592 3.2 12.1 1.0
CE1 B:HIS592 3.2 12.7 1.0
CE1 B:HIS433 3.3 12.2 1.0
CB B:HIS592 3.4 9.8 1.0
ND1 B:HIS431 4.2 6.8 1.0
CG B:HIS431 4.2 6.8 1.0
CG B:HIS433 4.2 10.0 1.0
NE2 B:HIS592 4.3 13.2 1.0
CD2 B:HIS592 4.3 12.6 1.0
ND1 B:HIS433 4.3 10.3 1.0
O B:HOH1005 4.3 17.0 1.0
O B:HOH1006 4.4 11.7 1.0
O2 B:TPQ382 4.7 20.6 1.0
SD B:MET602 4.9 20.1 1.0
CE B:MET602 4.9 17.8 1.0
CA B:HIS592 4.9 10.5 1.0

Reference:

S.Kishishita, T.Okajima, M.Kim, H.Yamaguchi, S.Hirota, S.Suzuki, S.Kuroda, K.Tanizawa, M.Mure. Role of Copper Ion in Bacterial Copper Amine Oxidase: Spectroscopic and Crystallographic Studies of Metal-Substituted Enzymes J.Am.Chem.Soc. V. 125 1041 2003.
ISSN: ISSN 0002-7863
PubMed: 12537504
DOI: 10.1021/JA017899K
Page generated: Sun Dec 13 10:59:29 2020

Last articles

Zn in 7O75
Zn in 7O73
Zn in 7O4I
Zn in 7O72
Zn in 7O4J
Zn in 7NVR
Zn in 7NVY
Zn in 7NVZ
Zn in 7NW0
Zn in 7O4K
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy