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Copper in PDB 1d6z: Crystal Structure of the Aerobically Freeze Trapped Rate-Determining Catalytic Intermediate of E. Coli Copper-Containing Amine Oxidase.

Enzymatic activity of Crystal Structure of the Aerobically Freeze Trapped Rate-Determining Catalytic Intermediate of E. Coli Copper-Containing Amine Oxidase.

All present enzymatic activity of Crystal Structure of the Aerobically Freeze Trapped Rate-Determining Catalytic Intermediate of E. Coli Copper-Containing Amine Oxidase.:
1.4.3.6;

Protein crystallography data

The structure of Crystal Structure of the Aerobically Freeze Trapped Rate-Determining Catalytic Intermediate of E. Coli Copper-Containing Amine Oxidase., PDB code: 1d6z 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 / 2.10
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 (%) 19.3 / 23.7

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of the Aerobically Freeze Trapped Rate-Determining Catalytic Intermediate of E. Coli Copper-Containing Amine Oxidase. (pdb code 1d6z). 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 the Aerobically Freeze Trapped Rate-Determining Catalytic Intermediate of E. Coli Copper-Containing Amine Oxidase., PDB code: 1d6z:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1d6z

Go back to Copper Binding Sites List in 1d6z
Copper binding site 1 out of 2 in the Crystal Structure of the Aerobically Freeze Trapped Rate-Determining Catalytic Intermediate of E. Coli Copper-Containing Amine Oxidase.


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 the Aerobically Freeze Trapped Rate-Determining Catalytic Intermediate of E. Coli Copper-Containing Amine Oxidase. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu801

b:24.6
occ:1.00
NE2 A:HIS526 2.0 22.9 1.0
NE2 A:HIS524 2.2 25.4 1.0
ND1 A:HIS689 2.2 23.1 1.0
O1 A:PEO2002 2.7 50.9 1.0
CD2 A:HIS526 2.8 20.3 1.0
O2 A:PEO2002 3.0 44.1 1.0
CE1 A:HIS524 3.0 21.9 1.0
CE1 A:HIS526 3.2 22.7 1.0
CE1 A:HIS689 3.2 20.8 1.0
CG A:HIS689 3.2 21.2 1.0
CD2 A:HIS524 3.2 22.8 1.0
CB A:HIS689 3.4 20.9 1.0
O A:HOH2573 3.8 35.6 1.0
CG A:HIS526 4.0 23.8 1.0
ND1 A:HIS526 4.2 24.5 1.0
ND1 A:HIS524 4.2 20.2 1.0
NE2 A:HIS689 4.3 19.6 1.0
CG A:HIS524 4.3 22.2 1.0
CD2 A:HIS689 4.3 19.4 1.0
OZ A:TYY466 4.7 39.8 1.0
O A:HOH2438 4.7 24.9 1.0
CE A:MET699 4.8 30.0 1.0
SD A:MET699 4.9 33.8 1.0
CA A:HIS689 5.0 22.0 1.0
CE1 A:HIS613 5.0 24.1 1.0

Copper binding site 2 out of 2 in 1d6z

Go back to Copper Binding Sites List in 1d6z
Copper binding site 2 out of 2 in the Crystal Structure of the Aerobically Freeze Trapped Rate-Determining Catalytic Intermediate of E. Coli Copper-Containing Amine Oxidase.


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 the Aerobically Freeze Trapped Rate-Determining Catalytic Intermediate of E. Coli Copper-Containing Amine Oxidase. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu801

b:23.9
occ:1.00
NE2 B:HIS526 2.1 25.2 1.0
NE2 B:HIS524 2.1 26.2 1.0
ND1 B:HIS689 2.2 21.0 1.0
O1 B:PEO3002 2.8 40.6 1.0
CD2 B:HIS526 2.8 18.8 1.0
CE1 B:HIS524 2.9 22.9 1.0
O2 B:PEO3002 3.0 35.0 1.0
CG B:HIS689 3.1 21.4 1.0
CD2 B:HIS524 3.2 23.6 1.0
CE1 B:HIS689 3.2 18.7 1.0
CE1 B:HIS526 3.2 24.2 1.0
CB B:HIS689 3.4 22.4 1.0
ND1 B:HIS524 4.1 23.9 1.0
CG B:HIS526 4.1 22.4 1.0
CG B:HIS524 4.2 25.3 1.0
ND1 B:HIS526 4.2 24.2 1.0
CD2 B:HIS689 4.3 19.4 1.0
NE2 B:HIS689 4.3 20.2 1.0
OE2 B:GLU490 4.8 51.0 1.0
O B:HOH3047 4.8 32.6 1.0
OZ B:TYY466 4.8 40.6 1.0
CA B:HIS689 4.9 22.4 1.0
SD B:MET699 4.9 39.0 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 21:40:17 2020
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