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

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

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

Protein crystallography data

The structure of Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Early Intermediate in Topaquinone Biogenesis, PDB code: 1ivv 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 / 2.10
Space group I 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 157.802, 63.069, 183.461, 90.00, 111.64, 90.00
R / Rfree (%) 19 / 26.3

Copper Binding Sites:

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

Copper binding site 1 out of 2 in 1ivv

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

b:26.1
occ:1.00
NE2 A:HIS431 1.9 10.0 1.0
NE2 A:HIS433 2.0 26.3 1.0
O A:HOH1005 2.1 67.2 1.0
ND1 A:HIS592 2.2 15.0 0.8
ND1 A:HIS592 2.2 17.1 0.2
OZ A:DAH382 2.6 25.2 1.0
CE1 A:HIS431 2.9 8.6 1.0
CE1 A:HIS433 3.0 19.4 1.0
CD2 A:HIS431 3.0 7.7 1.0
CD2 A:HIS433 3.0 18.8 1.0
CG A:HIS592 3.1 15.2 0.2
CG A:HIS592 3.1 16.6 0.8
CE1 A:HIS592 3.2 14.7 0.8
CE1 A:HIS592 3.2 16.0 0.2
CZ A:DAH382 3.4 20.6 1.0
CB A:HIS592 3.4 16.3 1.0
ND1 A:HIS431 4.0 8.2 1.0
CE1 A:DAH382 4.0 24.9 1.0
CG A:HIS431 4.1 6.6 1.0
ND1 A:HIS433 4.1 13.0 1.0
CG A:HIS433 4.2 20.7 1.0
CE2 A:DAH382 4.2 21.4 1.0
O A:HOH1002 4.3 14.7 1.0
CD2 A:HIS592 4.3 17.4 0.2
CD2 A:HIS592 4.3 13.2 0.8
NE2 A:HIS592 4.3 18.9 0.2
NE2 A:HIS592 4.3 15.0 0.8
OE2 A:DAH382 4.3 25.9 0.5
SD A:MET602 4.8 29.4 1.0
CA A:HIS592 4.9 12.2 1.0
CE A:MET602 5.0 31.6 1.0

Copper binding site 2 out of 2 in 1ivv

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

b:25.4
occ:1.00
O B:HOH1474 1.9 51.9 1.0
ND1 B:HIS592 2.0 15.9 0.8
NE2 B:HIS431 2.0 11.4 1.0
NE2 B:HIS433 2.1 23.6 1.0
ND1 B:HIS592 2.2 14.0 0.2
CG B:HIS592 2.8 13.3 0.8
CG B:HIS592 2.8 13.9 0.2
CB B:HIS592 2.9 17.4 1.0
CD2 B:HIS433 3.0 15.2 1.0
CE1 B:HIS431 3.0 6.5 1.0
CD2 B:HIS431 3.0 10.0 1.0
OZ B:DAH382 3.1 24.0 1.0
CE1 B:HIS433 3.2 11.4 1.0
CE1 B:HIS592 3.2 13.8 0.8
CE1 B:HIS592 3.4 14.4 0.2
CZ B:DAH382 3.8 17.9 1.0
CD2 B:HIS592 4.0 14.5 0.8
O B:HOH1473 4.1 59.2 1.0
ND1 B:HIS431 4.1 6.5 1.0
CE1 B:DAH382 4.1 19.4 1.0
CG B:HIS431 4.2 8.9 1.0
CD2 B:HIS592 4.2 14.4 0.2
CG B:HIS433 4.2 14.3 1.0
NE2 B:HIS592 4.2 16.3 0.8
ND1 B:HIS433 4.3 14.3 1.0
NE2 B:HIS592 4.4 14.2 0.2
CA B:HIS592 4.4 17.3 1.0
CE2 B:DAH382 4.6 15.4 1.0
CE B:MET602 4.6 26.2 1.0
SD B:MET602 4.6 22.2 1.0
O B:HOH1475 4.8 13.7 1.0
OE2 B:DAH382 4.9 17.6 0.5

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

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