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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

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