Atomistry » Copper » PDB 1oe2-1rjp » 1ui8
Atomistry »
  Copper »
    PDB 1oe2-1rjp »
      1ui8 »

Copper in PDB 1ui8: Site-Directed Mutagenesis of HIS592 Involved in Binding of Copper Ion in Arthrobacter Globiformis Amine Oxidase

Enzymatic activity of Site-Directed Mutagenesis of HIS592 Involved in Binding of Copper Ion in Arthrobacter Globiformis Amine Oxidase

All present enzymatic activity of Site-Directed Mutagenesis of HIS592 Involved in Binding of Copper Ion in Arthrobacter Globiformis Amine Oxidase:
1.4.3.6;

Protein crystallography data

The structure of Site-Directed Mutagenesis of HIS592 Involved in Binding of Copper Ion in Arthrobacter Globiformis Amine Oxidase, PDB code: 1ui8 was solved by H.Matsunami, T.Okajima, S.Hirota, H.Yamaguchi, H.Hori, S.Kuroda, K.Tanizawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.80
Space group I 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 157.762, 63.210, 184.244, 90.00, 111.64, 90.00
R / Rfree (%) 21.7 / 25.8

Copper Binding Sites:

The binding sites of Copper atom in the Site-Directed Mutagenesis of HIS592 Involved in Binding of Copper Ion in Arthrobacter Globiformis Amine Oxidase (pdb code 1ui8). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Site-Directed Mutagenesis of HIS592 Involved in Binding of Copper Ion in Arthrobacter Globiformis Amine Oxidase, PDB code: 1ui8:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1ui8

Go back to Copper Binding Sites List in 1ui8
Copper binding site 1 out of 2 in the Site-Directed Mutagenesis of HIS592 Involved in Binding of Copper Ion in Arthrobacter Globiformis Amine Oxidase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Site-Directed Mutagenesis of HIS592 Involved in Binding of Copper Ion in Arthrobacter Globiformis Amine Oxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1001

b:2.0
occ:1.00
O4 A:TPQ382 1.9 38.3 1.0
NE2 A:HIS431 2.2 9.3 1.0
NE2 A:HIS433 2.3 17.9 1.0
O5 A:TPQ382 2.6 40.8 1.0
C4 A:TPQ382 2.8 37.4 1.0
CD2 A:HIS433 3.1 16.9 1.0
C5 A:TPQ382 3.1 37.7 1.0
CE1 A:HIS431 3.2 8.7 1.0
CD2 A:HIS431 3.2 5.1 1.0
CE1 A:HIS433 3.4 16.9 1.0
C3 A:TPQ382 4.1 37.3 1.0
O A:HOH1185 4.1 14.2 1.0
ND1 A:HIS431 4.3 9.2 1.0
CB A:ALA592 4.3 11.7 1.0
CG A:HIS433 4.3 14.8 1.0
CG A:HIS431 4.3 7.0 1.0
C6 A:TPQ382 4.4 34.1 1.0
ND1 A:HIS433 4.4 16.0 1.0
CE A:MET602 4.6 25.2 1.0
SD A:MET602 4.7 24.9 1.0

Copper binding site 2 out of 2 in 1ui8

Go back to Copper Binding Sites List in 1ui8
Copper binding site 2 out of 2 in the Site-Directed Mutagenesis of HIS592 Involved in Binding of Copper Ion in Arthrobacter Globiformis Amine Oxidase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Site-Directed Mutagenesis of HIS592 Involved in Binding of Copper Ion in Arthrobacter Globiformis Amine Oxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1002

b:2.0
occ:1.00
O4 B:TPQ382 2.0 36.8 1.0
NE2 B:HIS431 2.2 9.7 1.0
NE2 B:HIS433 2.4 19.0 1.0
O5 B:TPQ382 2.4 37.6 1.0
C4 B:TPQ382 2.8 33.5 1.0
C5 B:TPQ382 3.0 34.7 1.0
CD2 B:HIS433 3.1 16.1 1.0
CD2 B:HIS431 3.2 6.5 1.0
CE1 B:HIS431 3.2 6.5 1.0
CE1 B:HIS433 3.5 17.6 1.0
C3 B:TPQ382 4.1 32.3 1.0
O B:HOH1105 4.1 13.3 1.0
CB B:ALA592 4.3 9.5 1.0
ND1 B:HIS431 4.3 8.6 1.0
CG B:HIS431 4.3 7.7 1.0
CG B:HIS433 4.4 13.5 1.0
C6 B:TPQ382 4.4 31.1 1.0
CE B:MET602 4.5 25.1 1.0
ND1 B:HIS433 4.5 16.4 1.0
O B:HOH1435 4.5 45.1 1.0
SD B:MET602 4.6 22.8 1.0

Reference:

H.Matsunami, T.Okajima, S.Hirota, H.Yamaguchi, H.Hori, S.Kuroda, K.Tanizawa. Chemical Rescue of A Site-Specific Mutant of Bacterial Copper Amine Oxidase For Generation of the Topa Quinone Cofactor Biochemistry V. 43 2178 2004.
ISSN: ISSN 0006-2960
PubMed: 14979714
DOI: 10.1021/BI0361923
Page generated: Thu Sep 3 16:21:27 2020
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy