Atomistry » Copper » PDB 1hc1-1jvo » 1ivu
Atomistry »
  Copper »
    PDB 1hc1-1jvo »
      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: Sun Dec 13 10:59:31 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy