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Copper in PDB 1oac: Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution

Enzymatic activity of Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution

All present enzymatic activity of Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution:
1.4.3.6;

Protein crystallography data

The structure of Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution, PDB code: 1oac was solved by M.R.Parsons, M.A.Convery, C.M.Wilmot, S.E.V.Phillips, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 135.732, 167.775, 81.904, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution (pdb code 1oac). 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 A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution, PDB code: 1oac:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1oac

Go back to Copper Binding Sites List in 1oac
Copper binding site 1 out of 2 in the Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution


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 A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu801

b:20.0
occ:1.00
 NE2 A:HIS526 2.0 19.1 1.0
ND1 A:HIS689 2.0 19.5 1.0
NE2 A:HIS524 2.0 17.9 1.0
O4 A:TPQ466 2.0 25.8 1.0
CE1 A:HIS526 2.9 26.9 1.0
CD2 A:HIS524 3.0 8.9 1.0
CE1 A:HIS689 3.0 18.2 1.0
CE1 A:HIS524 3.0 11.8 1.0
C4 A:TPQ466 3.0 45.9 1.0
CG A:HIS689 3.1 17.3 1.0
CD2 A:HIS526 3.1 24.0 1.0
CB A:HIS689 3.5 14.0 1.0
C3 A:TPQ466 3.5 45.1 1.0
ND1 A:HIS526 4.1 27.0 1.0
C5 A:TPQ466 4.1 46.2 1.0
NE2 A:HIS689 4.1 18.3 1.0
ND1 A:HIS524 4.1 11.1 1.0
CG A:HIS524 4.1 11.3 1.0
CD2 A:HIS689 4.2 16.3 1.0
CG A:HIS526 4.2 20.0 1.0
O A:HOH911 4.2 20.6 1.0
O5 A:TPQ466 4.3 47.9 1.0
O A:HOH980 4.4 51.6 1.0
C2 A:TPQ466 4.8 47.2 1.0
CG A:GLU490 5.0 38.8 1.0

Copper binding site 2 out of 2 in 1oac

Go back to Copper Binding Sites List in 1oac
Copper binding site 2 out of 2 in the Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution


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 A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu801

b:19.4
occ:1.00
 NE2 B:HIS526 2.0 17.3 1.0
ND1 B:HIS689 2.0 17.4 1.0
O4 B:TPQ466 2.0 23.2 1.0
NE2 B:HIS524 2.0 18.6 1.0
CE1 B:HIS526 2.8 27.9 1.0
CE1 B:HIS689 2.9 12.5 1.0
CE1 B:HIS524 2.9 10.4 1.0
C4 B:TPQ466 3.0 41.3 1.0
CD2 B:HIS524 3.1 11.8 1.0
CG B:HIS689 3.1 14.8 1.0
CD2 B:HIS526 3.1 24.4 1.0
C3 B:TPQ466 3.5 40.3 1.0
CB B:HIS689 3.5 15.7 1.0
ND1 B:HIS526 4.0 29.8 1.0
ND1 B:HIS524 4.1 16.1 1.0
NE2 B:HIS689 4.1 10.9 1.0
C5 B:TPQ466 4.1 45.2 1.0
CD2 B:HIS689 4.2 9.7 1.0
CG B:HIS524 4.2 17.1 1.0
CG B:HIS526 4.2 21.4 1.0
O B:HOH1192 4.3 43.1 1.0
O5 B:TPQ466 4.4 49.0 1.0
O B:HOH988 4.4 44.5 1.0
O B:HOH923 4.4 23.0 1.0
C2 B:TPQ466 4.8 44.0 1.0
SD B:MET699 5.0 29.9 1.0

Reference:

M.R.Parsons, M.A.Convery, C.M.Wilmot, K.D.Yadav, V.Blakeley, A.S.Corner, S.E.Phillips, M.J.Mcpherson, P.F.Knowles. Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 A Resolution. Structure V. 3 1171 1995.
ISSN: ISSN 0969-2126
PubMed: 8591028
DOI: 10.1016/S0969-2126(01)00253-2
Page generated: Thu Sep 3 16:11:51 2020
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