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Copper in PDB 3qjs: The Structure of and Photolytic Induced Changes of Carbon Monoxide Binding to the Cytochrome BA3-Oxidase From Thermus Thermophilus

Enzymatic activity of The Structure of and Photolytic Induced Changes of Carbon Monoxide Binding to the Cytochrome BA3-Oxidase From Thermus Thermophilus

All present enzymatic activity of The Structure of and Photolytic Induced Changes of Carbon Monoxide Binding to the Cytochrome BA3-Oxidase From Thermus Thermophilus:
1.9.3.1;

Protein crystallography data

The structure of The Structure of and Photolytic Induced Changes of Carbon Monoxide Binding to the Cytochrome BA3-Oxidase From Thermus Thermophilus, PDB code: 3qjs was solved by B.Liu, Y.Zhang, J.T.Sage, T.Doukov, Y.Chen, C.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 (°) 114.206, 114.206, 146.934, 90.00, 90.00, 90.00
R / Rfree (%) 21.5 / 26.5

Other elements in 3qjs:

The structure of The Structure of and Photolytic Induced Changes of Carbon Monoxide Binding to the 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 The Structure of and Photolytic Induced Changes of Carbon Monoxide Binding to the Cytochrome BA3-Oxidase From Thermus Thermophilus (pdb code 3qjs). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the The Structure of and Photolytic Induced Changes of Carbon Monoxide Binding to the Cytochrome BA3-Oxidase From Thermus Thermophilus, PDB code: 3qjs:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 3qjs

Go back to Copper Binding Sites List in 3qjs
Copper binding site 1 out of 3 in the The Structure of and Photolytic Induced Changes of Carbon Monoxide Binding to the 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 The Structure of and Photolytic Induced Changes of Carbon Monoxide Binding to the Cytochrome BA3-Oxidase From Thermus Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu803

b:41.6
occ:1.00
 NE2 A:HIS282 2.1 50.4 1.0
ND1 A:HIS233 2.1 52.3 1.0
NE2 A:HIS283 2.2 50.5 1.0
O A:CMO563 2.3 36.4 1.0
CE1 A:HIS282 2.8 52.4 1.0
CG A:HIS233 3.0 51.1 1.0
C A:CMO563 3.0 46.2 1.0
CD2 A:HIS283 3.0 48.6 1.0
CE1 A:HIS233 3.1 52.0 1.0
CE1 A:HIS283 3.2 50.9 1.0
CB A:HIS233 3.2 51.5 1.0
CD2 A:HIS282 3.3 53.1 1.0
CA A:HIS233 3.6 51.8 1.0
ND1 A:HIS282 4.0 53.4 1.0
CD2 A:HIS233 4.2 53.7 1.0
CG A:HIS283 4.2 48.1 1.0
NE2 A:HIS233 4.2 53.5 1.0
ND1 A:HIS283 4.2 51.7 1.0
ND A:HAS801 4.3 36.8 1.0
CG A:HIS282 4.3 52.5 1.0
C1D A:HAS801 4.5 39.5 1.0
C4D A:HAS801 4.5 36.2 1.0
N A:HIS233 4.5 52.8 1.0
C A:HIS233 4.6 52.6 1.0
O A:HIS233 4.7 51.8 1.0
C2D A:HAS801 4.7 41.9 1.0
C3D A:HAS801 4.8 38.9 1.0
FE A:HAS801 5.0 37.6 1.0
CG2 A:VAL236 5.0 43.3 1.0
O A:GLY232 5.0 52.9 1.0
CHB A:HAS801 5.0 37.5 1.0

Copper binding site 2 out of 3 in 3qjs

Go back to Copper Binding Sites List in 3qjs
Copper binding site 2 out of 3 in the The Structure of and Photolytic Induced Changes of Carbon Monoxide Binding to the 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 The Structure of and Photolytic Induced Changes of Carbon Monoxide Binding to the Cytochrome BA3-Oxidase From Thermus Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu802

b:42.7
occ:1.00
 CU1 B:CUA802 0.0 42.7 1.0
ND1 B:HIS157 1.9 50.0 1.0
SG B:CYS149 2.3 45.4 1.0
SG B:CYS153 2.4 52.5 1.0
O B:GLN151 2.6 52.4 1.0
CU2 B:CUA802 2.6 41.5 1.0
CE1 B:HIS157 2.7 43.5 1.0
CG B:HIS157 3.1 51.5 1.0
C B:GLN151 3.5 50.5 1.0
CB B:CYS149 3.6 48.4 1.0
CB B:HIS157 3.6 54.0 1.0
N B:CYS153 3.7 52.0 1.0
CB B:CYS153 3.7 53.4 1.0
CA B:HIS157 3.8 54.2 1.0
O B:CYS149 3.9 47.4 1.0
NE2 B:HIS157 3.9 48.3 1.0
CD2 B:HIS157 4.1 49.3 1.0
C B:TYR152 4.1 51.7 1.0
N B:GLN151 4.1 48.6 1.0
CA B:TYR152 4.2 50.7 1.0
C B:CYS149 4.2 47.3 1.0
N B:TYR152 4.3 50.3 1.0
CA B:CYS153 4.3 53.4 1.0
O B:HIS157 4.4 53.8 1.0
CA B:GLN151 4.4 49.7 1.0
ND1 B:HIS114 4.4 47.5 1.0
SD B:MET160 4.5 54.6 1.0
C B:HIS157 4.5 54.5 1.0
CA B:CYS149 4.6 47.3 1.0
CB B:MET160 4.8 52.2 1.0
N B:ASN150 4.9 46.8 1.0
O B:TYR152 4.9 51.8 1.0

Copper binding site 3 out of 3 in 3qjs

Go back to Copper Binding Sites List in 3qjs
Copper binding site 3 out of 3 in the The Structure of and Photolytic Induced Changes of Carbon Monoxide Binding to the 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 The Structure of and Photolytic Induced Changes of Carbon Monoxide Binding to the Cytochrome BA3-Oxidase From Thermus Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu802

b:41.5
occ:1.00
 CU2 B:CUA802 0.0 41.5 1.0
ND1 B:HIS114 2.0 47.5 1.0
SG B:CYS149 2.4 45.4 1.0
SD B:MET160 2.4 54.6 1.0
SG B:CYS153 2.5 52.5 1.0
CU1 B:CUA802 2.6 42.7 1.0
CE1 B:HIS114 2.9 50.0 1.0
CG B:HIS114 3.1 48.0 1.0
CE B:MET160 3.2 53.2 1.0
CB B:CYS149 3.4 48.4 1.0
CB B:HIS114 3.5 48.0 1.0
CB B:CYS153 3.6 53.4 1.0
CG B:MET160 3.8 52.3 1.0
CA B:HIS114 4.0 47.9 1.0
NE2 B:HIS114 4.0 51.2 1.0
CD2 B:HIS114 4.2 48.5 1.0
O B:GLN151 4.2 52.4 1.0
CB B:MET160 4.2 52.2 1.0
ND1 B:HIS157 4.5 50.0 1.0
O B:ILE113 4.6 50.3 1.0
N B:GLY115 4.8 46.7 1.0
CA B:CYS149 4.8 47.3 1.0
O B:PHE86 4.9 55.9 1.0
CD2 B:PHE88 4.9 55.6 1.0
CA B:CYS153 4.9 53.4 1.0
C B:HIS114 5.0 47.4 1.0

Reference:

B.Liu, Y.Zhang, J.T.Sage, S.M.Soltis, T.Doukov, Y.Chen, C.D.Stout, J.A.Fee. Structural Changes That Occur Upon Photolysis of the Fe(II)(A3)-Co Complex in the Cytochrome Ba(3)-Oxidase of Thermus Thermophilus: A Combined X-Ray Crystallographic and Infrared Spectral Study Demonstrates Co Binding to Cu(B). Biochim.Biophys.Acta V.1817 658 2012.
ISSN: ISSN 0006-3002
PubMed: 22226917
DOI: 10.1016/J.BBABIO.2011.12.010
Page generated: Mon Jul 14 02:38:23 2025

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