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Copper in PDB 1d6y: Crystal Structure of E. Coli Copper-Containing Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine and Complexed with Nitric Oxide.

Enzymatic activity of Crystal Structure of E. Coli Copper-Containing Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine and Complexed with Nitric Oxide.

All present enzymatic activity of Crystal Structure of E. Coli Copper-Containing Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine and Complexed with Nitric Oxide.:
1.4.3.6;

Protein crystallography data

The structure of Crystal Structure of E. Coli Copper-Containing Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine and Complexed with Nitric Oxide., PDB code: 1d6y was solved by C.M.Wilmot, J.Hajdu, M.J.Mcpherson, P.F.Knowles, S.E.V.Phillips, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 135.236, 166.482, 79.628, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 23.1

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of E. Coli Copper-Containing Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine and Complexed with Nitric Oxide. (pdb code 1d6y). 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 E. Coli Copper-Containing Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine and Complexed with Nitric Oxide., PDB code: 1d6y:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1d6y

Go back to Copper Binding Sites List in 1d6y
Copper binding site 1 out of 2 in the Crystal Structure of E. Coli Copper-Containing Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine and Complexed with Nitric Oxide.


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 E. Coli Copper-Containing Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine and Complexed with Nitric Oxide. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu801

b:43.7
occ:1.00
NE2 A:HIS526 2.1 37.4 1.0
ND1 A:HIS689 2.1 37.8 1.0
NE2 A:HIS524 2.2 38.0 1.0
N A:NO2002 2.5 60.3 1.0
CD2 A:HIS526 2.8 36.1 1.0
CE1 A:HIS524 3.0 35.1 1.0
CG A:HIS689 3.1 37.1 1.0
CE1 A:HIS689 3.1 37.5 1.0
O A:NO2002 3.2 60.4 1.0
CD2 A:HIS524 3.3 34.5 1.0
CE1 A:HIS526 3.3 35.3 1.0
CB A:HIS689 3.4 35.0 1.0
CG A:HIS526 4.0 36.2 1.0
O A:HOH2573 4.1 53.5 1.0
ND1 A:HIS524 4.1 35.3 1.0
ND1 A:HIS526 4.2 36.7 1.0
NE2 A:HIS689 4.2 36.7 1.0
CD2 A:HIS689 4.3 35.9 1.0
CG A:HIS524 4.3 35.6 1.0
O A:HOH2435 4.8 49.1 1.0
SD A:MET699 4.8 45.1 1.0
CE A:MET699 4.9 45.2 1.0
CA A:HIS689 4.9 34.2 1.0
CE1 A:HIS613 5.0 39.4 1.0

Copper binding site 2 out of 2 in 1d6y

Go back to Copper Binding Sites List in 1d6y
Copper binding site 2 out of 2 in the Crystal Structure of E. Coli Copper-Containing Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine and Complexed with Nitric Oxide.


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 E. Coli Copper-Containing Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine and Complexed with Nitric Oxide. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu801

b:40.7
occ:1.00
NE2 B:HIS526 2.1 39.4 1.0
ND1 B:HIS689 2.1 31.6 1.0
NE2 B:HIS524 2.2 36.8 1.0
N B:NO3002 2.3 49.7 1.0
O B:NO3002 3.0 48.1 1.0
CE1 B:HIS524 3.0 36.5 1.0
CD2 B:HIS526 3.0 35.9 1.0
CE1 B:HIS689 3.1 32.5 1.0
CG B:HIS689 3.1 33.7 1.0
CE1 B:HIS526 3.2 38.5 1.0
CD2 B:HIS524 3.2 36.9 1.0
CB B:HIS689 3.5 33.7 1.0
ND1 B:HIS524 4.1 37.8 1.0
CG B:HIS526 4.2 35.7 1.0
NE2 B:HIS689 4.2 34.6 1.0
ND1 B:HIS526 4.2 37.9 1.0
CG B:HIS524 4.3 36.8 1.0
CD2 B:HIS689 4.3 32.5 1.0
OE2 B:GLU490 4.6 59.1 1.0
O B:HOH3043 4.7 42.6 1.0
SD B:MET699 4.8 49.4 1.0
CA B:HIS689 5.0 33.5 1.0
CE B:MET699 5.0 47.0 1.0

Reference:

C.M.Wilmot, J.Hajdu, M.J.Mcpherson, P.F.Knowles, S.E.Phillips. Visualization of Dioxygen Bound to Copper During Enzyme Catalysis. Science V. 286 1724 1999.
ISSN: ISSN 0036-8075
PubMed: 10576737
DOI: 10.1126/SCIENCE.286.5445.1724
Page generated: Wed Sep 2 21:40:09 2020
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