Atomistry » Copper » PDB 1eso-1haw » 1ivu
Atomistry »
  Copper »
    PDB 1eso-1haw »
      1ivu »

Copper in PDB 1ivu: Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Initial Intermediate in Topaquinone Biogenesis

Enzymatic activity of Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Initial Intermediate in Topaquinone Biogenesis

All present enzymatic activity of Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Initial Intermediate in Topaquinone Biogenesis:
1.4.3.6;

Protein crystallography data

The structure of Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Initial Intermediate in Topaquinone Biogenesis, PDB code: 1ivu was solved by M.Kim, T.Okajima, S.Kishishita, M.Yoshimura, A.Kawamori, K.Tanizawa, H.Yamaguchi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.00 / 1.90
Space group I 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 157.878, 63.176, 184.279, 90.00, 111.81, 90.00
R / Rfree (%) 19.9 / 25.8

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Initial Intermediate in Topaquinone Biogenesis (pdb code 1ivu). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Initial Intermediate in Topaquinone Biogenesis, PDB code: 1ivu:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1ivu

Go back to Copper Binding Sites List in 1ivu
Copper binding site 1 out of 2 in the Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Initial Intermediate in Topaquinone Biogenesis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Initial Intermediate in Topaquinone Biogenesis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1001

b:19.1
occ:1.00
NE2 A:HIS431 1.8 2.0 1.0
ND1 A:HIS592 2.1 21.3 0.3
NE2 A:HIS433 2.1 23.0 1.0
ND1 A:HIS592 2.2 18.9 0.7
OH A:TYR382 2.6 27.3 1.0
CE1 A:HIS431 2.8 9.2 1.0
CD2 A:HIS431 2.8 6.2 1.0
CD2 A:HIS433 3.0 18.9 1.0
CE1 A:HIS592 3.0 26.2 0.3
CE1 A:HIS592 3.1 22.3 0.7
CG A:HIS592 3.2 28.0 0.3
CG A:HIS592 3.2 24.8 0.7
CE1 A:HIS433 3.2 17.3 1.0
CZ A:TYR382 3.3 21.0 1.0
CB A:HIS592 3.5 21.9 1.0
ND1 A:HIS431 3.9 7.0 1.0
CE2 A:TYR382 3.9 23.6 1.0
CG A:HIS431 4.0 6.3 1.0
CE1 A:TYR382 4.0 19.2 1.0
NE2 A:HIS592 4.2 24.4 0.3
CG A:HIS433 4.2 20.5 1.0
NE2 A:HIS592 4.2 18.3 0.7
O A:HOH1002 4.3 13.2 1.0
CD2 A:HIS592 4.3 22.7 0.7
CD2 A:HIS592 4.3 28.2 0.3
ND1 A:HIS433 4.3 17.9 1.0
SD A:MET602 4.9 33.0 1.0

Copper binding site 2 out of 2 in 1ivu

Go back to Copper Binding Sites List in 1ivu
Copper binding site 2 out of 2 in the Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Initial Intermediate in Topaquinone Biogenesis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Initial Intermediate in Topaquinone Biogenesis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1002

b:19.5
occ:1.00
NE2 B:HIS431 2.0 10.9 1.0
ND1 B:HIS592 2.0 23.1 0.7
NE2 B:HIS433 2.1 23.5 1.0
ND1 B:HIS592 2.5 26.2 0.3
CD2 B:HIS431 2.7 13.3 1.0
OH B:TYR382 2.8 22.5 1.0
CD2 B:HIS433 2.9 22.2 1.0
CG B:HIS592 3.0 18.0 0.7
CE1 B:HIS592 3.0 23.8 0.7
CE1 B:HIS431 3.1 10.5 1.0
CE1 B:HIS433 3.2 17.4 1.0
CG B:HIS592 3.3 23.3 0.3
CB B:HIS592 3.3 26.9 1.0
CE1 B:HIS592 3.6 24.4 0.3
CZ B:TYR382 3.6 20.6 1.0
CG B:HIS431 3.9 8.2 1.0
ND1 B:HIS431 4.0 13.1 1.0
NE2 B:HIS592 4.1 23.2 0.7
CD2 B:HIS592 4.1 23.4 0.7
CG B:HIS433 4.1 18.5 1.0
ND1 B:HIS433 4.2 14.7 1.0
CE2 B:TYR382 4.2 18.9 1.0
CE1 B:TYR382 4.3 20.0 1.0
O B:HOH1104 4.5 19.2 1.0
CD2 B:HIS592 4.5 25.3 0.3
NE2 B:HIS592 4.6 24.2 0.3
CA B:HIS592 4.8 19.2 1.0
CE B:MET602 4.8 28.7 1.0
SD B:MET602 4.9 29.6 1.0

Reference:

M.Kim, T.Okajima, S.Kishishita, M.Yoshimura, A.Kawamori, K.Tanizawa, H.Yamaguchi. X-Ray Snapshots of Quinone Cofactor Biogenesis in Bacterial Copper Amine Oxidase. Nat.Struct.Biol. V. 9 591 2002.
ISSN: ISSN 1072-8368
PubMed: 12134140
DOI: 10.1038/NSB824
Page generated: Thu Sep 3 16:00:19 2020
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy