Atomistry » Copper » PDB 2pp8-2vr6 » 2qpe
Atomistry »
  Copper »
    PDB 2pp8-2vr6 »
      2qpe »

Copper in PDB 2qpe: An Unexpected Outcome of Surface-Engineering An Integral Membrane Protein: Improved Crystallization of Cytochrome BA3 Oxidase From Thermus Thermophilus

Enzymatic activity of An Unexpected Outcome of Surface-Engineering An Integral Membrane Protein: Improved Crystallization of Cytochrome BA3 Oxidase From Thermus Thermophilus

All present enzymatic activity of An Unexpected Outcome of Surface-Engineering An Integral Membrane Protein: Improved Crystallization of Cytochrome BA3 Oxidase From Thermus Thermophilus:
1.9.3.1;

Protein crystallography data

The structure of An Unexpected Outcome of Surface-Engineering An Integral Membrane Protein: Improved Crystallization of Cytochrome BA3 Oxidase From Thermus Thermophilus, PDB code: 2qpe was solved by B.Liu, V.M.Luna, 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) 19.99 / 2.90
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 114.635, 114.635, 148.568, 90.00, 90.00, 90.00
R / Rfree (%) 23.4 / 30.2

Other elements in 2qpe:

The structure of An Unexpected Outcome of Surface-Engineering An Integral Membrane Protein: Improved Crystallization 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 An Unexpected Outcome of Surface-Engineering An Integral Membrane Protein: Improved Crystallization of Cytochrome BA3 Oxidase From Thermus Thermophilus (pdb code 2qpe). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the An Unexpected Outcome of Surface-Engineering An Integral Membrane Protein: Improved Crystallization of Cytochrome BA3 Oxidase From Thermus Thermophilus, PDB code: 2qpe:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 2qpe

Go back to Copper Binding Sites List in 2qpe
Copper binding site 1 out of 3 in the An Unexpected Outcome of Surface-Engineering An Integral Membrane Protein: Improved Crystallization 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 An Unexpected Outcome of Surface-Engineering An Integral Membrane Protein: Improved Crystallization of Cytochrome BA3 Oxidase From Thermus Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu803

b:84.0
occ:1.00
 NE2 A:HIS282 1.9 76.8 1.0
ND1 A:HIS233 2.0 84.8 1.0
NE2 A:HIS283 2.1 76.6 1.0
CE1 A:HIS282 2.7 71.8 1.0
CE1 A:HIS233 2.7 93.9 1.0
CD2 A:HIS283 2.8 81.6 1.0
CG A:HIS233 3.0 81.1 1.0
CD2 A:HIS282 3.1 90.0 1.0
CE1 A:HIS283 3.2 79.0 1.0
CB A:HIS233 3.5 80.1 1.0
NE2 A:HIS233 3.8 86.5 1.0
ND1 A:HIS282 3.9 72.5 1.0
CD2 A:HIS233 3.9 86.6 1.0
ND A:HAS801 4.0 76.7 1.0
CA A:HIS233 4.0 81.8 1.0
CG A:HIS283 4.1 82.5 1.0
C1D A:HAS801 4.1 87.0 1.0
C4D A:HAS801 4.1 80.4 1.0
CG A:HIS282 4.1 82.6 1.0
ND1 A:HIS283 4.2 82.7 1.0
C2D A:HAS801 4.4 73.7 1.0
C3D A:HAS801 4.4 74.9 1.0
FE A:HAS801 4.6 77.5 1.0
CHA A:HAS801 4.7 70.3 1.0
CHB A:HAS801 4.7 75.5 1.0
C1A A:HAS801 4.8 75.1 1.0
NA A:HAS801 4.9 83.2 1.0
OMD A:HAS801 4.9 70.4 1.0
C A:HIS233 4.9 85.2 1.0
NB A:HAS801 5.0 73.8 1.0

Copper binding site 2 out of 3 in 2qpe

Go back to Copper Binding Sites List in 2qpe
Copper binding site 2 out of 3 in the An Unexpected Outcome of Surface-Engineering An Integral Membrane Protein: Improved Crystallization 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 An Unexpected Outcome of Surface-Engineering An Integral Membrane Protein: Improved Crystallization of Cytochrome BA3 Oxidase From Thermus Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu802

b:90.4
occ:1.00
 CU1 B:CUA802 0.0 90.4 1.0
SG B:CYS153 2.0 81.2 1.0
ND1 B:HIS157 2.0 83.7 1.0
SG B:CYS149 2.2 69.5 1.0
O B:GLN151 2.4 88.5 1.0
CU2 B:CUA802 2.7 88.3 1.0
CE1 B:HIS157 2.7 79.3 1.0
CG B:HIS157 3.0 72.6 1.0
N B:CYS153 3.3 86.5 1.0
CB B:CYS153 3.3 85.5 1.0
C B:GLN151 3.4 83.2 1.0
CB B:HIS157 3.6 64.6 1.0
CB B:CYS149 3.8 65.0 1.0
NE2 B:HIS157 3.8 69.2 1.0
CA B:HIS157 3.8 73.1 1.0
CA B:CYS153 3.9 85.1 1.0
CA B:TYR152 3.9 84.5 1.0
C B:TYR152 3.9 86.7 1.0
CD2 B:HIS157 4.0 85.0 1.0
N B:TYR152 4.1 82.7 1.0
SD B:MET160 4.2 88.2 1.0
N B:GLN151 4.3 80.0 1.0
O B:HIS157 4.4 69.2 1.0
CA B:GLN151 4.5 79.5 1.0
C B:HIS157 4.5 73.4 1.0
ND1 B:HIS114 4.5 87.2 1.0
C B:CYS149 4.7 79.0 1.0
O B:CYS149 4.7 82.8 1.0
CB B:MET160 4.7 90.1 1.0
C B:CYS153 4.7 84.7 1.0
CA B:CYS149 4.9 71.1 1.0
CE2 B:PHE88 4.9 95.3 1.0
CB B:HIS114 5.0 74.6 1.0
O B:TYR152 5.0 91.5 1.0

Copper binding site 3 out of 3 in 2qpe

Go back to Copper Binding Sites List in 2qpe
Copper binding site 3 out of 3 in the An Unexpected Outcome of Surface-Engineering An Integral Membrane Protein: Improved Crystallization 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 An Unexpected Outcome of Surface-Engineering An Integral Membrane Protein: Improved Crystallization of Cytochrome BA3 Oxidase From Thermus Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu802

b:88.3
occ:1.00
 CU2 B:CUA802 0.0 88.3 1.0
SD B:MET160 2.1 88.2 1.0
ND1 B:HIS114 2.2 87.2 1.0
SG B:CYS153 2.2 81.2 1.0
SG B:CYS149 2.4 69.5 1.0
CU1 B:CUA802 2.7 90.4 1.0
CG B:HIS114 2.9 78.8 1.0
CB B:HIS114 3.0 74.6 1.0
CB B:CYS153 3.1 85.5 1.0
CE B:MET160 3.2 86.8 1.0
CE1 B:HIS114 3.3 89.2 1.0
CB B:CYS149 3.4 65.0 1.0
CG B:MET160 3.7 84.5 1.0
CA B:HIS114 3.8 79.8 1.0
O B:GLN151 4.0 88.5 1.0
CB B:MET160 4.0 90.1 1.0
CD2 B:HIS114 4.1 88.6 1.0
NE2 B:HIS114 4.2 88.4 1.0
ND1 B:HIS157 4.5 83.7 1.0
CA B:CYS153 4.5 85.1 1.0
CD2 B:PHE88 4.7 0.8 1.0
N B:GLY115 4.7 80.7 1.0
CE2 B:PHE88 4.7 95.3 1.0
N B:CYS153 4.7 86.5 1.0
N B:HIS114 4.8 82.5 1.0
CA B:CYS149 4.8 71.1 1.0
C B:HIS114 4.8 81.4 1.0
O B:ILE113 4.8 82.9 1.0

Reference:

B.Liu, V.M.Luna, Y.Chen, C.D.Stout, J.A.Fee. An Unexpected Outcome of Surface Engineering An Integral Membrane Protein: Improved Crystallization of Cytochrome Ba(3) From Thermus Thermophilus. Acta Crystallogr.,Sect.F V. 63 1029 2007.
ISSN: ESSN 1744-3091
PubMed: 18084085
DOI: 10.1107/S1744309107054176
Page generated: Wed Jul 31 00:00:39 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy