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Copper in PDB 1ivx: Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Holo Form Generated By Biogenesis in Crystal.

Enzymatic activity of Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Holo Form Generated By Biogenesis in Crystal.

All present enzymatic activity of Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Holo Form Generated By Biogenesis in Crystal.:
1.4.3.6;

Protein crystallography data

The structure of Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Holo Form Generated By Biogenesis in Crystal., PDB code: 1ivx 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) 10.00 / 2.20
Space group I 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 158.076, 63.390, 184.018, 90.00, 111.60, 90.00
R / Rfree (%) 21.7 / 29.2

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Holo Form Generated By Biogenesis in Crystal. (pdb code 1ivx). 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: Holo Form Generated By Biogenesis in Crystal., PDB code: 1ivx:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1ivx

Go back to Copper Binding Sites List in 1ivx
Copper binding site 1 out of 2 in the Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Holo Form Generated By Biogenesis in Crystal.


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: Holo Form Generated By Biogenesis in Crystal. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1001

b:10.3
occ:1.00
NE2 A:HIS431 1.9 3.7 1.0
O A:HOH1002 2.0 2.0 1.0
ND1 A:HIS592 2.1 19.6 1.0
NE2 A:HIS433 2.2 17.1 1.0
CD2 A:HIS431 2.9 2.6 1.0
O A:HOH1003 2.9 26.1 1.0
CE1 A:HIS431 3.0 2.0 1.0
CD2 A:HIS433 3.0 9.9 1.0
CG A:HIS592 3.0 19.9 1.0
CE1 A:HIS592 3.1 14.8 1.0
CB A:HIS592 3.2 17.8 1.0
CE1 A:HIS433 3.2 12.5 1.0
O A:HOH1578 3.8 27.9 1.0
ND1 A:HIS431 4.0 3.7 1.0
CG A:HIS431 4.0 2.0 1.0
CD2 A:HIS592 4.2 16.7 1.0
NE2 A:HIS592 4.2 17.4 1.0
CG A:HIS433 4.2 13.8 1.0
ND1 A:HIS433 4.3 12.2 1.0
O A:HOH1004 4.3 10.3 1.0
O2 A:TPQ382 4.4 24.6 1.0
O A:HOH1005 4.4 23.7 1.0
CA A:HIS592 4.8 17.7 1.0
CE A:MET602 4.8 26.0 1.0
SD A:MET602 4.9 22.8 1.0

Copper binding site 2 out of 2 in 1ivx

Go back to Copper Binding Sites List in 1ivx
Copper binding site 2 out of 2 in the Crystal Structure of Copper Amine Oxidase From Arthrobacter Globiformis: Holo Form Generated By Biogenesis in Crystal.


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: Holo Form Generated By Biogenesis in Crystal. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1002

b:9.1
occ:1.00
O B:HOH1659 2.0 4.8 1.0
NE2 B:HIS431 2.0 5.9 1.0
ND1 B:HIS592 2.0 18.1 1.0
NE2 B:HIS433 2.2 17.9 1.0
CD2 B:HIS433 2.9 10.9 1.0
CD2 B:HIS431 3.0 5.0 1.0
O B:HOH1003 3.0 16.3 1.0
CG B:HIS592 3.0 18.3 1.0
CE1 B:HIS592 3.0 16.5 1.0
CE1 B:HIS431 3.1 2.0 1.0
CE1 B:HIS433 3.3 11.6 1.0
CB B:HIS592 3.3 16.9 1.0
O B:HOH1444 4.0 43.6 1.0
CG B:HIS431 4.1 3.4 1.0
ND1 B:HIS431 4.1 2.0 1.0
NE2 B:HIS592 4.1 15.6 1.0
CG B:HIS433 4.1 13.9 1.0
CD2 B:HIS592 4.2 19.6 1.0
ND1 B:HIS433 4.3 12.2 1.0
O2 B:TPQ382 4.4 16.4 0.8
O B:HOH1004 4.4 5.5 1.0
O B:HOH1349 4.7 21.3 1.0
CE B:MET602 4.7 29.5 1.0
CA B:HIS592 4.9 13.8 1.0
O B:HOH1006 4.9 26.1 1.0
SD B:MET602 4.9 19.6 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 16:00:45 2020
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