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Copper in PDB 1qal: 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: 1qal 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 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 135.050, 166.520, 79.320, 90.00, 90.00, 90.00
R / Rfree (%) 19.2 / 24.1

Other elements in 1qal:

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 1qal). 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: 1qal:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1qal

Go back to Copper Binding Sites List in 1qal
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:30.5
occ:1.00
 NE2 A:HIS526 2.1 22.4 1.0
NE2 A:HIS524 2.3 25.6 1.0
ND1 A:HIS689 2.3 22.9 1.0
O A:HOH1574 2.6 30.7 1.0
CD2 A:HIS526 2.9 23.7 1.0
CE1 A:HIS524 3.0 17.1 1.0
CE1 A:HIS526 3.2 26.3 1.0
CD2 A:HIS524 3.2 17.9 1.0
CG A:HIS689 3.3 20.3 1.0
CE1 A:HIS689 3.3 20.2 1.0
CB A:HIS689 3.5 22.6 1.0
CG A:HIS526 4.1 23.5 1.0
ND1 A:HIS524 4.1 22.9 1.0
ND1 A:HIS526 4.2 29.4 1.0
O A:HOH1392 4.2 39.9 1.0
CG A:HIS524 4.3 22.9 1.0
O A:HOH973 4.3 53.1 1.0
CD2 A:HIS689 4.4 23.8 1.0
NE2 A:HIS689 4.4 23.6 1.0
O A:HOH1577 4.6 27.7 1.0
O2 A:TPQ466 4.7 52.6 1.0
SD A:MET699 4.8 37.4 1.0

Copper binding site 2 out of 2 in 1qal

Go back to Copper Binding Sites List in 1qal
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:26.6
occ:1.00
 NE2 B:HIS526 2.1 23.6 1.0
NE2 B:HIS524 2.2 25.0 1.0
ND1 B:HIS689 2.2 21.2 1.0
O B:HOH1535 2.5 31.8 1.0
CD2 B:HIS526 2.9 20.2 1.0
CE1 B:HIS524 2.9 18.1 1.0
CD2 B:HIS524 3.2 23.7 1.0
CG B:HIS689 3.2 22.5 1.0
CE1 B:HIS526 3.2 22.1 1.0
CE1 B:HIS689 3.2 22.1 1.0
CB B:HIS689 3.4 20.1 1.0
CG B:HIS526 4.0 25.7 1.0
ND1 B:HIS524 4.1 25.2 1.0
ND1 B:HIS526 4.2 29.2 1.0
CG B:HIS524 4.2 25.3 1.0
NE2 B:HIS689 4.3 28.6 1.0
O B:HOH1421 4.3 29.8 1.0
CD2 B:HIS689 4.3 20.3 1.0
O B:HOH855 4.4 23.9 1.0
O B:HOH1534 4.8 34.7 1.0
O2 B:TPQ466 4.8 48.8 1.0
SD B:MET699 4.9 39.5 1.0
CA B:HIS689 5.0 24.4 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: Tue Jul 30 22:37:11 2024

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