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Copper in PDB 3qjr: 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: 3qjr 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) 19.89 / 3.20
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 108.810, 108.810, 164.460, 90.00, 90.00, 90.00
R / Rfree (%) 31.8 / 36.7

Other elements in 3qjr:

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

Copper binding site 1 out of 3 in 3qjr

Go back to Copper Binding Sites List in 3qjr
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:22.4
occ:1.00
 NE2 A:HIS282 1.9 21.4 1.0
C A:CMO563 1.9 40.0 1.0
NE2 A:HIS283 1.9 23.1 1.0
ND1 A:HIS233 2.0 23.8 1.0
O A:CMO563 2.5 36.1 1.0
CE1 A:HIS283 2.6 23.4 1.0
CE1 A:HIS282 2.8 21.6 1.0
CE1 A:HIS233 2.9 23.2 1.0
CD2 A:HIS282 2.9 22.8 1.0
CG A:HIS233 3.0 24.0 1.0
CD2 A:HIS283 3.0 23.6 1.0
CB A:HIS233 3.3 24.1 1.0
ND1 A:HIS283 3.7 23.9 1.0
ND1 A:HIS282 3.9 21.8 1.0
CG A:HIS283 4.0 23.8 1.0
CA A:HIS233 4.0 24.2 1.0
NE2 A:HIS233 4.0 22.6 1.0
CG A:HIS282 4.0 22.7 1.0
CD2 A:HIS233 4.1 23.1 1.0
C1D A:HAS801 4.1 23.1 1.0
ND A:HAS801 4.1 23.4 1.0
C4D A:HAS801 4.4 23.6 1.0
C2D A:HAS801 4.4 23.8 1.0
CHB A:HAS801 4.4 23.4 1.0
C3D A:HAS801 4.6 24.2 1.0
FE A:HAS801 4.7 23.9 1.0
C1B A:HAS801 4.9 24.4 1.0
NB A:HAS801 4.9 24.4 1.0
C A:HIS233 5.0 24.3 1.0
N A:HIS233 5.0 24.2 1.0
OMD A:HAS801 5.0 24.6 1.0

Copper binding site 2 out of 3 in 3qjr

Go back to Copper Binding Sites List in 3qjr
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:16.8
occ:1.00
 CU1 B:CUA802 0.0 16.8 1.0
ND1 B:HIS157 1.9 24.3 1.0
SG B:CYS153 2.0 19.9 1.0
SG B:CYS149 2.1 22.2 1.0
O B:GLN151 2.6 24.5 1.0
CU2 B:CUA802 2.7 20.5 1.0
CG B:HIS157 2.9 24.0 1.0
CE1 B:HIS157 2.9 24.2 1.0
CB B:HIS157 3.2 23.8 1.0
CB B:CYS149 3.3 23.0 1.0
CB B:CYS153 3.4 22.0 1.0
N B:CYS153 3.4 22.7 1.0
C B:GLN151 3.6 24.0 1.0
CA B:HIS157 3.7 23.7 1.0
O B:HIS157 3.9 23.7 1.0
CA B:CYS153 4.0 22.3 1.0
CD2 B:HIS157 4.0 24.0 1.0
NE2 B:HIS157 4.0 24.0 1.0
O B:CYS149 4.1 23.1 1.0
C B:TYR152 4.1 22.9 1.0
CA B:TYR152 4.2 23.0 1.0
C B:HIS157 4.2 23.7 1.0
C B:CYS149 4.3 23.1 1.0
SD B:MET160 4.3 23.0 1.0
N B:TYR152 4.3 23.5 1.0
N B:GLN151 4.4 24.0 1.0
CA B:CYS149 4.4 23.0 1.0
ND1 B:HIS114 4.4 23.6 1.0
CA B:GLN151 4.6 24.0 1.0
CB B:MET160 4.8 23.1 1.0
N B:ASN150 4.9 23.2 1.0
C B:CYS153 5.0 22.5 1.0

Copper binding site 3 out of 3 in 3qjr

Go back to Copper Binding Sites List in 3qjr
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:20.5
occ:1.00
 CU2 B:CUA802 0.0 20.5 1.0
ND1 B:HIS114 2.0 23.6 1.0
SG B:CYS149 2.1 22.2 1.0
SG B:CYS153 2.2 19.9 1.0
SD B:MET160 2.3 23.0 1.0
CU1 B:CUA802 2.7 16.8 1.0
CE1 B:HIS114 2.9 23.6 1.0
CG B:HIS114 3.1 23.2 1.0
CB B:CYS149 3.2 23.0 1.0
CE B:MET160 3.2 23.7 1.0
CB B:CYS153 3.2 22.0 1.0
CB B:HIS114 3.5 23.5 1.0
CG B:MET160 3.9 23.4 1.0
CA B:HIS114 4.0 23.6 1.0
NE2 B:HIS114 4.1 22.8 1.0
O B:GLN151 4.1 24.5 1.0
CD2 B:HIS114 4.2 22.7 1.0
CB B:MET160 4.3 23.1 1.0
ND1 B:HIS157 4.6 24.3 1.0
CA B:CYS149 4.6 23.0 1.0
CA B:CYS153 4.6 22.3 1.0
O B:ILE113 4.7 23.7 1.0
N B:GLY115 4.7 23.7 1.0
N B:CYS153 4.9 22.7 1.0
C B:HIS114 5.0 23.7 1.0
O B:PHE86 5.0 23.0 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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