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

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

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

Protein crystallography data

The structure of Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Late Intermediate in Topaquinone Biogenesis, PDB code: 1ivw 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 / 1.80
Space group I 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 157.007, 62.896, 182.834, 90.00, 111.82, 90.00
R / Rfree (%) 21 / 26.2

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Late Intermediate in Topaquinone Biogenesis (pdb code 1ivw). 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: Late Intermediate in Topaquinone Biogenesis, PDB code: 1ivw:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1ivw

Go back to Copper Binding Sites List in 1ivw
Copper binding site 1 out of 2 in the Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Late 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: Late Intermediate in Topaquinone Biogenesis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1001

b:14.8
occ:1.00
NE2 A:HIS431 1.9 3.8 1.0
ND1 A:HIS592 2.0 16.2 1.0
NE2 A:HIS433 2.1 14.8 1.0
O4 A:TPQ382 2.7 21.2 1.0
CD2 A:HIS431 2.9 4.9 1.0
CE1 A:HIS431 2.9 6.3 1.0
CD2 A:HIS433 2.9 10.0 1.0
CG A:HIS592 3.0 16.4 1.0
CE1 A:HIS592 3.1 20.2 1.0
CE1 A:HIS433 3.2 12.3 1.0
CB A:HIS592 3.3 13.1 1.0
O A:HOH1006 3.4 28.7 1.0
C4 A:TPQ382 3.4 18.8 1.0
O5 A:TPQ382 3.8 31.5 1.0
C5 A:TPQ382 3.9 21.0 1.0
ND1 A:HIS431 4.0 7.2 1.0
CG A:HIS431 4.0 5.7 1.0
CG A:HIS433 4.1 14.3 1.0
CD2 A:HIS592 4.2 15.3 1.0
NE2 A:HIS592 4.2 16.3 1.0
C3 A:TPQ382 4.3 15.3 1.0
ND1 A:HIS433 4.3 8.8 1.0
O A:HOH1005 4.3 38.5 1.0
O A:HOH1002 4.4 12.9 1.0
SD A:MET602 4.8 19.2 1.0
CA A:HIS592 4.8 13.0 1.0

Copper binding site 2 out of 2 in 1ivw

Go back to Copper Binding Sites List in 1ivw
Copper binding site 2 out of 2 in the Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Late 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: Late Intermediate in Topaquinone Biogenesis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1002

b:18.5
occ:1.00
NE2 B:HIS431 2.0 10.4 1.0
ND1 B:HIS592 2.1 21.1 1.0
NE2 B:HIS433 2.1 15.2 1.0
CD2 B:HIS433 3.0 10.9 1.0
O4 B:TPQ382 3.0 18.8 1.0
CE1 B:HIS431 3.0 10.1 1.0
CD2 B:HIS431 3.0 10.7 1.0
CG B:HIS592 3.1 17.6 1.0
CE1 B:HIS592 3.1 20.7 1.0
CE1 B:HIS433 3.3 14.0 1.0
CB B:HIS592 3.4 12.8 1.0
C4 B:TPQ382 3.6 18.2 1.0
O5 B:TPQ382 4.0 28.6 1.0
ND1 B:HIS431 4.1 11.2 1.0
C5 B:TPQ382 4.1 14.7 1.0
CG B:HIS431 4.2 10.9 1.0
CG B:HIS433 4.2 11.7 1.0
NE2 B:HIS592 4.3 18.6 1.0
CD2 B:HIS592 4.3 16.1 1.0
ND1 B:HIS433 4.3 12.1 1.0
O B:HOH1486 4.3 48.3 1.0
C3 B:TPQ382 4.4 18.7 1.0
SD B:MET602 4.6 20.8 1.0
O B:HOH1109 4.7 11.3 1.0
CE B:MET602 4.7 23.7 1.0
CA B:HIS592 5.0 15.1 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 16:00:31 2020
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