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Copper in PDB 1d6u: Crystal Structure of E. Coli Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine

Enzymatic activity of Crystal Structure of E. Coli Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine

All present enzymatic activity of Crystal Structure of E. Coli Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine:
1.4.3.6;

Protein crystallography data

The structure of Crystal Structure of E. Coli Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine, PDB code: 1d6u 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 / 23.9

Other elements in 1d6u:

The structure of Crystal Structure of E. Coli Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of E. Coli Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine (pdb code 1d6u). 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 Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine, PDB code: 1d6u:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1d6u

Go back to Copper Binding Sites List in 1d6u
Copper binding site 1 out of 2 in the Crystal Structure of E. Coli Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine


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 Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu801

b:26.5
occ:1.00
NE2 A:HIS526 2.1 21.9 1.0
NE2 A:HIS524 2.1 28.2 1.0
ND1 A:HIS689 2.2 22.6 1.0
CD2 A:HIS526 2.8 23.8 1.0
O A:HOH2440 2.9 27.1 1.0
CE1 A:HIS524 2.9 21.2 1.0
CG A:HIS689 3.2 19.0 1.0
CE1 A:HIS526 3.2 27.7 1.0
CE1 A:HIS689 3.2 20.2 1.0
CD2 A:HIS524 3.3 20.6 1.0
CB A:HIS689 3.4 22.6 1.0
O A:HOH2589 3.8 44.3 1.0
CG A:HIS526 4.0 21.8 1.0
ND1 A:HIS524 4.1 24.8 1.0
ND1 A:HIS526 4.2 29.4 1.0
CG A:HIS524 4.3 22.6 1.0
NE2 A:HIS689 4.3 23.6 1.0
CD2 A:HIS689 4.4 19.6 1.0
O A:HOH2756 4.6 39.6 1.0
OZ A:TYQ466 4.8 44.4 1.0
O A:HOH2448 4.8 34.4 1.0
SD A:MET699 4.8 50.8 1.0
CE A:MET699 4.9 52.3 1.0
CE1 A:HIS613 5.0 25.7 1.0
CA A:HIS689 5.0 21.2 1.0

Copper binding site 2 out of 2 in 1d6u

Go back to Copper Binding Sites List in 1d6u
Copper binding site 2 out of 2 in the Crystal Structure of E. Coli Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine


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 Amine Oxidase Anaerobically Reduced with Beta-Phenylethylamine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu801

b:29.4
occ:1.00
NE2 B:HIS526 2.1 31.1 1.0
ND1 B:HIS689 2.2 19.2 1.0
NE2 B:HIS524 2.2 24.6 1.0
O B:HOH3413 2.8 21.2 1.0
CD2 B:HIS526 2.9 25.8 1.0
CE1 B:HIS524 3.0 22.3 1.0
CG B:HIS689 3.1 22.7 1.0
CE1 B:HIS526 3.2 28.6 1.0
CE1 B:HIS689 3.2 18.4 1.0
CD2 B:HIS524 3.2 26.2 1.0
CB B:HIS689 3.3 18.2 1.0
CG B:HIS526 4.1 22.6 1.0
ND1 B:HIS524 4.1 25.5 1.0
O B:HOH3179 4.2 40.8 1.0
ND1 B:HIS526 4.2 27.6 1.0
CG B:HIS524 4.3 26.4 1.0
CD2 B:HIS689 4.3 18.1 1.0
NE2 B:HIS689 4.3 23.3 1.0
SD B:MET699 4.8 53.0 1.0
O B:HOH3037 4.8 35.3 1.0
CA B:HIS689 4.9 22.4 1.0
OZ B:TYQ466 4.9 45.9 1.0
O B:HOH3695 5.0 23.4 1.0
OE2 B:GLU490 5.0 60.7 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 Oct 28 14:14:07 2020
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