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Copper in PDB 1qak: The Active Site Base Controls Cofactor Reactivity in Escherichia Coli Amine Oxidase : X-Ray Crystallographic Studies with Mutational Variants

Enzymatic activity of The Active Site Base Controls Cofactor Reactivity in Escherichia Coli Amine Oxidase : X-Ray Crystallographic Studies with Mutational Variants

All present enzymatic activity of The Active Site Base Controls Cofactor Reactivity in Escherichia Coli Amine Oxidase : X-Ray Crystallographic Studies with Mutational Variants:
1.4.3.4;

Protein crystallography data

The structure of The Active Site Base Controls Cofactor Reactivity in Escherichia Coli Amine Oxidase : X-Ray Crystallographic Studies with Mutational Variants, PDB code: 1qak was solved by J.M.Murray, C.M.Wilmot, C.G.Saysell, J.Jaeger, P.F.Knowles, S.E.Phillips, M.J.Mcpherson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 134.660, 166.170, 79.090, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 24.4

Other elements in 1qak:

The structure of The Active Site Base Controls Cofactor Reactivity in Escherichia Coli Amine Oxidase : X-Ray Crystallographic Studies with Mutational Variants also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Copper Binding Sites:

The binding sites of Copper atom in the The Active Site Base Controls Cofactor Reactivity in Escherichia Coli Amine Oxidase : X-Ray Crystallographic Studies with Mutational Variants (pdb code 1qak). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the The Active Site Base Controls Cofactor Reactivity in Escherichia Coli Amine Oxidase : X-Ray Crystallographic Studies with Mutational Variants, PDB code: 1qak:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1qak

Go back to Copper Binding Sites List in 1qak
Copper binding site 1 out of 2 in the The Active Site Base Controls Cofactor Reactivity in Escherichia Coli Amine Oxidase : X-Ray Crystallographic Studies with Mutational Variants


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of The Active Site Base Controls Cofactor Reactivity in Escherichia Coli Amine Oxidase : X-Ray Crystallographic Studies with Mutational Variants within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu801

b:26.2
occ:1.00
 NE2 A:HIS526 2.1 21.5 1.0
ND1 A:HIS689 2.2 16.2 1.0
NE2 A:HIS524 2.3 21.3 1.0
O4 A:TPQ466 2.5 43.1 0.8
O A:HOH1574 2.9 69.4 0.5
CD2 A:HIS526 2.9 23.7 1.0
CE1 A:HIS524 3.1 19.2 1.0
CE1 A:HIS526 3.1 25.1 1.0
CG A:HIS689 3.2 17.6 1.0
CE1 A:HIS689 3.2 19.1 1.0
CD2 A:HIS524 3.2 20.2 1.0
C4 A:TPQ466 3.4 48.8 0.8
CB A:HIS689 3.4 17.0 1.0
O A:HOH964 3.9 34.9 1.0
O5 A:TPQ466 3.9 53.6 0.8
C5 A:TPQ466 4.0 53.5 0.8
CG A:HIS526 4.1 23.8 1.0
ND1 A:HIS526 4.1 25.5 1.0
ND1 A:HIS524 4.2 21.7 1.0
C3 A:TPQ466 4.3 50.5 0.8
NE2 A:HIS689 4.3 20.0 1.0
CG A:HIS524 4.3 20.0 1.0
CD2 A:HIS689 4.3 21.4 1.0
O2 A:TPQ466 4.5 46.4 0.2
O A:HOH1306 4.5 35.2 1.0
CE1 A:HIS613 4.8 20.7 1.0
SD A:MET699 4.9 39.4 1.0
CE A:MET699 4.9 34.9 1.0
CA A:HIS689 5.0 16.7 1.0

Copper binding site 2 out of 2 in 1qak

Go back to Copper Binding Sites List in 1qak
Copper binding site 2 out of 2 in the The Active Site Base Controls Cofactor Reactivity in Escherichia Coli Amine Oxidase : X-Ray Crystallographic Studies with Mutational Variants


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of The Active Site Base Controls Cofactor Reactivity in Escherichia Coli Amine Oxidase : X-Ray Crystallographic Studies with Mutational Variants within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu801

b:23.3
occ:1.00
 NE2 B:HIS526 2.2 22.9 1.0
ND1 B:HIS689 2.2 16.6 1.0
NE2 B:HIS524 2.2 23.8 1.0
O4 B:TPQ466 2.4 39.7 0.8
CD2 B:HIS526 3.1 24.3 1.0
CE1 B:HIS524 3.1 20.5 1.0
CE1 B:HIS526 3.2 30.4 1.0
CD2 B:HIS524 3.2 23.2 1.0
CG B:HIS689 3.2 15.3 1.0
CE1 B:HIS689 3.2 19.5 1.0
C4 B:TPQ466 3.3 49.3 0.8
CB B:HIS689 3.4 14.9 1.0
O B:HOH1503 3.7 67.5 0.5
C3 B:TPQ466 4.0 50.5 0.8
O B:HOH1267 4.1 35.5 1.0
C5 B:TPQ466 4.2 54.1 0.8
CG B:HIS526 4.2 24.2 1.0
ND1 B:HIS524 4.2 26.3 1.0
O5 B:TPQ466 4.2 50.2 0.8
ND1 B:HIS526 4.2 28.4 1.0
CG B:HIS524 4.3 23.4 1.0
NE2 B:HIS689 4.3 18.2 1.0
CD2 B:HIS689 4.3 15.0 1.0
O B:HOH926 4.5 25.9 1.0
SD B:MET699 4.7 33.5 1.0
NE2 B:HIS613 4.8 26.6 1.0
O2 B:TPQ466 4.9 53.7 0.2
CA B:HIS689 4.9 18.9 1.0

Reference:

J.M.Murray, C.G.Saysell, C.M.Wilmot, W.S.Tambyrajah, J.Jaeger, P.F.Knowles, S.E.Phillips, M.J.Mcpherson. The Active Site Base Controls Cofactor Reactivity in Escherichia Coli Amine Oxidase: X-Ray Crystallographic Studies with Mutational Variants. Biochemistry V. 38 8217 1999.
ISSN: ISSN 0006-2960
PubMed: 10387067
DOI: 10.1021/BI9900469
Page generated: Mon Jul 14 00:18:31 2025

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