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Copper in PDB 1xme: Structure of Recombinant Cytochrome BA3 Oxidase From Thermus Thermophilus

Enzymatic activity of Structure of Recombinant Cytochrome BA3 Oxidase From Thermus Thermophilus

All present enzymatic activity of Structure of Recombinant Cytochrome BA3 Oxidase From Thermus Thermophilus:
1.9.3.1;

Protein crystallography data

The structure of Structure of Recombinant Cytochrome BA3 Oxidase From Thermus Thermophilus, PDB code: 1xme was solved by L.M.Hunsicker-Wang, R.L.Pacoma, Y.Chen, J.A.Fee, C.D.Stout, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 21.42 / 2.30
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 114.902, 114.902, 177.064, 90.00, 90.00, 90.00
R / Rfree (%) 21.7 / 23.6

Other elements in 1xme:

The structure of Structure of Recombinant 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 Recombinant Cytochrome BA3 Oxidase From Thermus Thermophilus (pdb code 1xme). 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 Recombinant Cytochrome BA3 Oxidase From Thermus Thermophilus, PDB code: 1xme:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 1xme

Go back to Copper Binding Sites List in 1xme
Copper binding site 1 out of 3 in the Structure of Recombinant 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 Recombinant Cytochrome BA3 Oxidase From Thermus Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu803

b:38.5
occ:1.00
ND1 A:HIS233 2.0 34.4 1.0
NE2 A:HIS282 2.0 40.8 1.0
NE2 A:HIS283 2.0 40.8 1.0
O A:HOH867 2.1 29.2 1.0
CE1 A:HIS283 2.8 38.5 1.0
CE1 A:HIS282 2.8 42.1 1.0
CG A:HIS233 2.9 32.1 1.0
CE1 A:HIS233 3.0 34.0 1.0
CD2 A:HIS283 3.0 39.5 1.0
CD2 A:HIS282 3.1 41.0 1.0
CB A:HIS233 3.3 31.6 1.0
CA A:HIS233 3.8 31.9 1.0
ND1 A:HIS283 3.9 38.7 1.0
ND A:HAS801 3.9 38.9 1.0
ND1 A:HIS282 4.0 39.8 1.0
CG A:HIS283 4.0 40.0 1.0
NE2 A:HIS233 4.1 35.6 1.0
CD2 A:HIS233 4.1 32.3 1.0
C1D A:HAS801 4.1 39.4 1.0
CG A:HIS282 4.1 42.6 1.0
C4D A:HAS801 4.2 38.6 1.0
FE A:HAS801 4.4 39.9 1.0
C2D A:HAS801 4.5 41.0 1.0
C3D A:HAS801 4.5 40.4 1.0
CHB A:HAS801 4.5 39.2 1.0
CHA A:HAS801 4.7 35.6 1.0
NB A:HAS801 4.7 39.4 1.0
N A:HIS233 4.8 32.3 1.0
C A:HIS233 4.8 32.2 1.0
NA A:HAS801 4.8 37.6 1.0
C1B A:HAS801 4.8 39.1 1.0
O A:HIS233 4.9 33.3 1.0
C1A A:HAS801 4.9 35.0 1.0

Copper binding site 2 out of 3 in 1xme

Go back to Copper Binding Sites List in 1xme
Copper binding site 2 out of 3 in the Structure of Recombinant 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 Recombinant Cytochrome BA3 Oxidase From Thermus Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu802

b:47.9
occ:1.00
CU1 B:CUA802 0.0 47.9 1.0
ND1 B:HIS157 2.1 35.0 1.0
SG B:CYS149 2.4 42.6 1.0
SG B:CYS153 2.4 40.0 1.0
CU2 B:CUA802 2.5 44.9 1.0
O B:GLN151 2.8 43.5 1.0
CE1 B:HIS157 3.1 37.3 1.0
CG B:HIS157 3.1 39.0 1.0
CB B:CYS149 3.4 47.1 1.0
CB B:HIS157 3.5 43.4 1.0
CB B:CYS153 3.6 40.6 1.0
C B:GLN151 3.6 43.7 1.0
N B:CYS153 3.6 43.2 1.0
CA B:HIS157 3.8 46.1 1.0
O B:HIS157 4.0 45.1 1.0
C B:TYR152 4.1 44.2 1.0
O B:CYS149 4.1 45.6 1.0
NE2 B:HIS157 4.2 39.0 1.0
CA B:TYR152 4.2 42.7 1.0
N B:TYR152 4.2 41.9 1.0
N B:GLN151 4.2 46.7 1.0
CA B:CYS153 4.2 43.0 1.0
CD2 B:HIS157 4.2 38.0 1.0
ND1 B:HIS114 4.3 32.4 1.0
C B:CYS149 4.3 47.8 1.0
C B:HIS157 4.3 46.9 1.0
CA B:CYS149 4.5 48.9 1.0
CA B:GLN151 4.5 45.0 1.0
SD B:MET160 4.5 45.8 1.0
CB B:MET160 4.7 50.0 1.0
O B:TYR152 5.0 43.4 1.0
N B:ASN150 5.0 47.6 1.0
O B:HOH814 5.0 52.5 1.0

Copper binding site 3 out of 3 in 1xme

Go back to Copper Binding Sites List in 1xme
Copper binding site 3 out of 3 in the Structure of Recombinant 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 Recombinant Cytochrome BA3 Oxidase From Thermus Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu802

b:44.9
occ:1.00
CU2 B:CUA802 0.0 44.9 1.0
ND1 B:HIS114 2.0 32.4 1.0
SG B:CYS153 2.3 40.0 1.0
SG B:CYS149 2.5 42.6 1.0
CU1 B:CUA802 2.5 47.9 1.0
SD B:MET160 2.6 45.8 1.0
CE1 B:HIS114 2.8 30.6 1.0
CE B:MET160 3.2 45.2 1.0
CG B:HIS114 3.2 35.9 1.0
CB B:CYS153 3.4 40.6 1.0
CB B:CYS149 3.5 47.1 1.0
CB B:HIS114 3.7 38.1 1.0
CG B:MET160 3.9 48.5 1.0
NE2 B:HIS114 4.0 32.5 1.0
CA B:HIS114 4.1 39.6 1.0
O B:GLN151 4.1 43.5 1.0
CD2 B:HIS114 4.2 31.9 1.0
CB B:MET160 4.2 50.0 1.0
ND1 B:HIS157 4.6 35.0 1.0
O B:ILE113 4.6 39.8 1.0
CA B:CYS153 4.7 43.0 1.0
O B:PHE86 4.8 45.2 1.0
N B:GLY115 4.8 41.1 1.0
N B:CYS153 4.9 43.2 1.0
CA B:CYS149 4.9 48.9 1.0

Reference:

L.M.Hunsicker-Wang, R.L.Pacoma, Y.Chen, J.A.Fee, C.D.Stout. A Novel Cryoprotection Scheme For Enhancing the Diffraction of Crystals of Recombinant Cytochrome BA3 Oxidase From Thermus Thermophilus. Acta Crystallogr.,Sect.D V. 61 340 2005.
ISSN: ISSN 0907-4449
PubMed: 15735345
DOI: 10.1107/S0907444904033906
Page generated: Sun Dec 13 11:03:02 2020

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