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Copper in PDB 3eh5: Structure of the Reduced Form of Cytochrome BA3 Oxidase From Thermus Thermophilus

Enzymatic activity of Structure of the Reduced Form of Cytochrome BA3 Oxidase From Thermus Thermophilus

All present enzymatic activity of Structure of the Reduced Form of Cytochrome BA3 Oxidase From Thermus Thermophilus:
1.9.3.1;

Protein crystallography data

The structure of Structure of the Reduced Form of Cytochrome BA3 Oxidase From Thermus Thermophilus, PDB code: 3eh5 was solved by B.Liu, Y.Chen, T.Doukov, S.M.Soltis, D.Stout, J.A.Fee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.80
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 115.631, 115.631, 149.169, 90.00, 90.00, 90.00
R / Rfree (%) 19.7 / 25.7

Other elements in 3eh5:

The structure of Structure of the Reduced Form of Cytochrome BA3 Oxidase From Thermus Thermophilus also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Structure of the Reduced Form of Cytochrome BA3 Oxidase From Thermus Thermophilus (pdb code 3eh5). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Structure of the Reduced Form of Cytochrome BA3 Oxidase From Thermus Thermophilus, PDB code: 3eh5:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 3eh5

Go back to Copper Binding Sites List in 3eh5
Copper binding site 1 out of 3 in the Structure of the Reduced Form of Cytochrome BA3 Oxidase From Thermus Thermophilus


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of the Reduced Form of Cytochrome BA3 Oxidase From Thermus Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu803

b:80.7
occ:1.00
NE2 A:HIS282 1.9 67.8 1.0
ND1 A:HIS233 2.2 84.7 1.0
NE2 A:HIS283 2.2 84.4 1.0
CE1 A:HIS282 2.8 66.9 1.0
CD2 A:HIS283 2.9 82.0 1.0
CD2 A:HIS282 3.1 74.5 1.0
CE1 A:HIS233 3.1 85.8 1.0
CG A:HIS233 3.2 79.8 1.0
CE1 A:HIS283 3.2 82.3 1.0
CB A:HIS233 3.4 75.5 1.0
CA A:HIS233 3.8 75.5 1.0
ND1 A:HIS282 4.0 69.2 1.0
CG A:HIS283 4.1 79.2 1.0
CG A:HIS282 4.1 72.8 1.0
ND1 A:HIS283 4.2 82.2 1.0
NE2 A:HIS233 4.2 82.5 1.0
CD2 A:HIS233 4.3 83.0 1.0
ND A:HAS801 4.3 68.6 1.0
C1D A:HAS801 4.3 72.6 1.0
C4D A:HAS801 4.4 66.2 1.0
C2D A:HAS801 4.5 67.8 1.0
C3D A:HAS801 4.5 66.0 1.0
C A:HIS233 4.8 76.7 1.0
N A:HIS233 4.8 77.0 1.0
O A:HIS233 4.9 75.3 1.0
CHB A:HAS801 4.9 71.9 1.0
CG2 A:VAL236 4.9 69.6 1.0
O A:GLY232 4.9 83.5 1.0
CHA A:HAS801 5.0 60.4 1.0

Copper binding site 2 out of 3 in 3eh5

Go back to Copper Binding Sites List in 3eh5
Copper binding site 2 out of 3 in the Structure of the Reduced Form of Cytochrome BA3 Oxidase From Thermus Thermophilus


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Structure of the Reduced Form of Cytochrome BA3 Oxidase From Thermus Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu802

b:80.3
occ:1.00
CU1 B:CUA802 0.0 80.3 1.0
ND1 B:HIS157 2.0 79.8 1.0
SG B:CYS153 2.4 80.3 1.0
SG B:CYS149 2.4 69.2 1.0
O B:GLN151 2.5 76.4 1.0
CU2 B:CUA802 2.7 80.5 1.0
CE1 B:HIS157 2.8 72.5 1.0
CG B:HIS157 3.2 80.6 1.0
C B:GLN151 3.5 74.1 1.0
CB B:CYS149 3.6 65.1 1.0
CB B:CYS153 3.7 78.1 1.0
O B:CYS149 3.8 69.1 1.0
CB B:HIS157 3.8 77.9 1.0
N B:CYS153 3.8 77.1 1.0
CA B:HIS157 3.9 77.1 1.0
NE2 B:HIS157 4.0 78.0 1.0
CA B:TYR152 4.1 76.9 1.0
N B:GLN151 4.2 69.8 1.0
C B:TYR152 4.2 78.0 1.0
N B:TYR152 4.2 74.9 1.0
CD2 B:HIS157 4.2 77.5 1.0
C B:CYS149 4.2 68.8 1.0
O B:HIS157 4.3 75.4 1.0
SD B:MET160 4.4 75.9 1.0
CA B:CYS153 4.4 78.0 1.0
C B:HIS157 4.5 76.3 1.0
CA B:GLN151 4.5 71.5 1.0
CA B:CYS149 4.6 66.4 1.0
ND1 B:HIS114 4.6 78.4 1.0
CB B:MET160 4.7 75.9 1.0
N B:ASN150 5.0 69.1 1.0

Copper binding site 3 out of 3 in 3eh5

Go back to Copper Binding Sites List in 3eh5
Copper binding site 3 out of 3 in the Structure of the Reduced Form of Cytochrome BA3 Oxidase From Thermus Thermophilus


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Structure of the Reduced Form of Cytochrome BA3 Oxidase From Thermus Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu802

b:80.5
occ:1.00
CU2 B:CUA802 0.0 80.5 1.0
ND1 B:HIS114 2.1 78.4 1.0
SG B:CYS153 2.5 80.3 1.0
SD B:MET160 2.5 75.9 1.0
SG B:CYS149 2.5 69.2 1.0
CU1 B:CUA802 2.7 80.3 1.0
CE1 B:HIS114 3.0 80.0 1.0
CG B:HIS114 3.2 78.2 1.0
CE B:MET160 3.2 77.5 1.0
CB B:CYS153 3.4 78.1 1.0
CB B:CYS149 3.6 65.1 1.0
CB B:HIS114 3.6 72.4 1.0
O B:GLN151 4.0 76.4 1.0
CG B:MET160 4.0 75.1 1.0
NE2 B:HIS114 4.1 78.0 1.0
CA B:HIS114 4.2 71.8 1.0
CD2 B:HIS114 4.3 78.4 1.0
CB B:MET160 4.3 75.9 1.0
O B:ILE113 4.6 70.4 1.0
ND1 B:HIS157 4.6 79.8 1.0
CD2 B:PHE88 4.8 80.5 1.0
CE2 B:PHE88 4.8 82.7 1.0
CA B:CYS153 4.8 78.0 1.0
N B:GLY115 4.9 74.0 1.0
O B:PHE86 4.9 71.3 1.0
CA B:CYS149 4.9 66.4 1.0

Reference:

B.Liu, Y.Chen, T.Doukov, S.M.Soltis, C.D.Stout, J.A.Fee. Combined Microspectrophotometric and Crystallographic Examination of Chemically Reduced and X-Ray Radiation-Reduced Forms of Cytochrome BA3 Oxidase From Thermus Thermophilus: Structure of the Reduced Form of the Enzyme. Biochemistry V. 48 820 2009.
ISSN: ISSN 0006-2960
PubMed: 19140675
DOI: 10.1021/BI801759A
Page generated: Wed Oct 28 14:23:44 2020
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