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Copper in PDB 3qjt: 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: 3qjt 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) 19.62 / 2.95
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 114.964, 114.964, 148.562, 90.00, 90.00, 90.00
R / Rfree (%) 25.8 / 32.3

Other elements in 3qjt:

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 3qjt). 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: 3qjt:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 3qjt

Go back to Copper Binding Sites List in 3qjt
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:57.0
occ:1.00
 ND1 A:HIS233 1.9 59.1 1.0
NE2 A:HIS282 2.0 60.1 1.0
NE2 A:HIS283 2.0 61.1 1.0
CE1 A:HIS233 2.5 59.1 1.0
CE1 A:HIS282 2.5 61.3 1.0
O A:CMO563 2.6 71.7 1.0
CG A:HIS233 2.7 59.3 1.0
CE1 A:HIS283 2.8 59.9 1.0
C A:CMO563 3.0 53.1 1.0
CD2 A:HIS283 3.0 61.1 1.0
CD2 A:HIS282 3.3 60.5 1.0
CB A:HIS233 3.3 60.3 1.0
NE2 A:HIS233 3.4 57.5 1.0
CD2 A:HIS233 3.5 58.4 1.0
ND1 A:HIS282 3.8 61.9 1.0
ND1 A:HIS283 3.9 61.5 1.0
CA A:HIS233 3.9 60.2 1.0
CG A:HIS283 4.0 60.5 1.0
CG A:HIS282 4.2 61.5 1.0
ND A:HAS801 4.4 52.0 1.0
C4D A:HAS801 4.5 50.6 1.0
C1D A:HAS801 4.5 54.7 1.0
C3D A:HAS801 4.8 52.2 1.0
C2D A:HAS801 4.8 54.9 1.0
N A:HIS233 4.8 61.2 1.0
C A:HIS233 4.9 60.3 1.0
O A:GLY232 4.9 60.2 1.0
CZ3 A:TRP229 4.9 64.5 1.0
CG2 A:VAL236 4.9 56.1 1.0
FE A:HAS801 4.9 48.6 1.0
O A:VAL279 4.9 62.2 1.0
O A:HIS233 5.0 59.5 1.0
NA A:HAS801 5.0 50.4 1.0
CG1 A:VAL236 5.0 56.9 1.0

Copper binding site 2 out of 3 in 3qjt

Go back to Copper Binding Sites List in 3qjt
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:56.8
occ:1.00
 CU1 B:CUA802 0.0 56.8 1.0
ND1 B:HIS157 2.0 61.3 1.0
O B:GLN151 2.2 60.8 1.0
SG B:CYS153 2.3 56.1 1.0
SG B:CYS149 2.3 57.7 1.0
CU2 B:CUA802 2.7 57.9 1.0
CE1 B:HIS157 2.9 59.9 1.0
CG B:HIS157 3.1 62.2 1.0
C B:GLN151 3.3 60.2 1.0
CB B:CYS149 3.5 58.4 1.0
CB B:HIS157 3.5 63.3 1.0
CB B:CYS153 3.6 61.2 1.0
CA B:HIS157 3.7 63.6 1.0
NE2 B:HIS157 4.0 61.3 1.0
O B:HIS157 4.0 62.8 1.0
N B:CYS153 4.0 61.3 1.0
N B:TYR152 4.0 60.2 1.0
CD2 B:HIS157 4.1 61.5 1.0
CA B:TYR152 4.1 60.5 1.0
N B:GLN151 4.1 58.8 1.0
O B:CYS149 4.1 58.8 1.0
C B:TYR152 4.2 60.8 1.0
C B:HIS157 4.2 63.5 1.0
SD B:MET160 4.2 59.1 1.0
CA B:GLN151 4.3 59.4 1.0
C B:CYS149 4.4 57.9 1.0
CA B:CYS153 4.5 61.7 1.0
CA B:CYS149 4.6 57.9 1.0
CB B:MET160 4.7 61.5 1.0
ND1 B:HIS114 4.8 60.6 1.0
O B:TYR152 4.9 60.6 1.0
N B:HIS157 4.9 64.6 1.0

Copper binding site 3 out of 3 in 3qjt

Go back to Copper Binding Sites List in 3qjt
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:57.9
occ:1.00
 CU2 B:CUA802 0.0 57.9 1.0
SG B:CYS149 2.3 57.7 1.0
ND1 B:HIS114 2.3 60.6 1.0
SD B:MET160 2.4 59.1 1.0
SG B:CYS153 2.5 56.1 1.0
CU1 B:CUA802 2.7 56.8 1.0
CG B:HIS114 3.2 59.7 1.0
CE1 B:HIS114 3.3 59.8 1.0
CE B:MET160 3.4 57.4 1.0
CB B:CYS149 3.4 58.4 1.0
CB B:CYS153 3.5 61.2 1.0
CB B:HIS114 3.5 59.1 1.0
O B:GLN151 3.7 60.8 1.0
CG B:MET160 3.9 60.5 1.0
CA B:HIS114 4.0 59.2 1.0
O B:ILE113 4.4 61.3 1.0
NE2 B:HIS114 4.4 59.1 1.0
CD2 B:HIS114 4.4 59.5 1.0
CB B:MET160 4.4 61.5 1.0
ND1 B:HIS157 4.7 61.3 1.0
CA B:CYS149 4.8 57.9 1.0
C B:GLN151 4.9 60.2 1.0
CA B:CYS153 4.9 61.7 1.0
N B:GLY115 4.9 58.1 1.0
CD2 B:PHE88 5.0 66.0 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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