Copper in PDB 1ehk: Crystal Structure of the Aberrant BA3-Cytochrome-C Oxidase From Thermus Thermophilus

All present enzymatic activity of Crystal Structure of the Aberrant BA3-Cytochrome-C Oxidase From Thermus Thermophilus:
1.9.3.1;

The structure of Crystal Structure of the Aberrant BA3-Cytochrome-C Oxidase From Thermus Thermophilus, PDB code: 1ehk was solved by T.Soulimane, G.Buse, G.P.Bourenkov, H.D.Bartunik, R.Huber, M.E.Than, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.40
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	112.110, 112.110, 161.410, 90.00, 90.00, 90.00
R / Rfree (%)	22.2 / 26.4

The structure of Crystal Structure of the Aberrant BA3-Cytochrome-C Oxidase From Thermus Thermophilus also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Copper atom in the Crystal Structure of the Aberrant BA3-Cytochrome-C Oxidase From Thermus Thermophilus (pdb code 1ehk). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Crystal Structure of the Aberrant BA3-Cytochrome-C Oxidase From Thermus Thermophilus, PDB code: 1ehk:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in the Crystal Structure of the Aberrant BA3-Cytochrome-C 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 Crystal Structure of the Aberrant BA3-Cytochrome-C Oxidase From Thermus Thermophilus within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu803 b:37.4 occ:1.00 ND1 A:HIS233 2.1 30.6 1.0 NE2 A:HIS283 2.1 32.3 1.0 NE2 A:HIS282 2.2 38.5 1.0 O A:HOH991 2.3 33.4 1.0 CE1 A:HIS283 2.8 26.4 1.0 CG A:HIS233 3.0 34.0 1.0 CE1 A:HIS282 3.0 35.7 1.0 CE1 A:HIS233 3.2 31.4 1.0 CB A:HIS233 3.2 25.0 1.0 CD2 A:HIS283 3.2 38.5 1.0 CD2 A:HIS282 3.3 31.0 1.0 CA A:HIS233 3.6 24.8 1.0 ND A:HAS801 3.9 29.7 1.0 C1D A:HAS801 4.0 32.5 1.0 ND1 A:HIS283 4.0 32.0 1.0 CG A:HIS283 4.2 36.9 1.0 C4D A:HAS801 4.2 30.7 1.0 NE2 A:HIS233 4.2 35.8 1.0 ND1 A:HIS282 4.2 34.1 1.0 CD2 A:HIS233 4.2 28.6 1.0 CG A:HIS282 4.3 34.2 1.0 C2D A:HAS801 4.4 29.3 1.0 FE A:HAS801 4.4 41.9 1.0 CHB A:HAS801 4.4 33.1 1.0 C3D A:HAS801 4.5 31.9 1.0 N A:HIS233 4.6 26.1 1.0 C A:HIS233 4.6 27.9 1.0 CHA A:HAS801 4.7 32.7 1.0 NB A:HAS801 4.7 44.7 1.0 O A:HIS233 4.7 26.0 1.0 C1B A:HAS801 4.8 40.5 1.0 NA A:HAS801 4.8 34.1 1.0 O A:GLY232 4.8 29.8 1.0 C1A A:HAS801 5.0 28.9 1.0

Copper binding site 2 out of 3 in the Crystal Structure of the Aberrant BA3-Cytochrome-C 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 Crystal Structure of the Aberrant BA3-Cytochrome-C Oxidase From Thermus Thermophilus within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu802 b:40.0 occ:1.00 CU1 B:CUA802 0.0 40.0 1.0 ND1 B:HIS157 2.1 26.7 1.0 SG B:CYS149 2.3 32.9 1.0 CU2 B:CUA802 2.4 40.6 1.0 SG B:CYS153 2.5 36.0 1.0 O B:GLN151 2.8 36.0 1.0 CE1 B:HIS157 3.0 29.1 1.0 CG B:HIS157 3.2 32.0 1.0 CB B:CYS153 3.4 25.4 1.0 CB B:CYS149 3.5 42.2 1.0 N B:CYS153 3.5 29.9 1.0 C B:GLN151 3.6 33.1 1.0 CB B:HIS157 3.7 36.3 1.0 CA B:HIS157 3.9 37.1 1.0 O B:CYS149 4.0 35.7 1.0 C B:TYR152 4.0 37.5 1.0 CA B:CYS153 4.1 32.0 1.0 NE2 B:HIS157 4.1 30.8 1.0 CA B:TYR152 4.2 34.5 1.0 N B:TYR152 4.2 28.9 1.0 N B:GLN151 4.2 42.5 1.0 O B:HIS157 4.3 38.9 1.0 ND1 B:HIS114 4.3 28.1 1.0 CD2 B:HIS157 4.3 31.0 1.0 SD B:MET160 4.3 41.4 1.0 C B:CYS149 4.4 38.2 1.0 CA B:GLN151 4.5 31.8 1.0 C B:HIS157 4.5 38.6 1.0 CA B:CYS149 4.6 41.4 1.0 CB B:MET160 4.8 47.0 1.0 O B:TYR152 4.9 35.1 1.0 O B:HOH806 5.0 42.9 1.0

Copper binding site 3 out of 3 in the Crystal Structure of the Aberrant BA3-Cytochrome-C 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 Crystal Structure of the Aberrant BA3-Cytochrome-C Oxidase From Thermus Thermophilus within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu802 b:40.6 occ:1.00 CU2 B:CUA802 0.0 40.6 1.0 ND1 B:HIS114 2.1 28.1 1.0 SG B:CYS153 2.4 36.0 1.0 SG B:CYS149 2.4 32.9 1.0 CU1 B:CUA802 2.4 40.0 1.0 SD B:MET160 2.5 41.4 1.0 CE1 B:HIS114 2.9 28.8 1.0 CB B:CYS153 3.2 25.4 1.0 CG B:HIS114 3.3 27.9 1.0 CB B:CYS149 3.4 42.2 1.0 CE B:MET160 3.5 35.8 1.0 CB B:HIS114 3.9 33.0 1.0 CG B:MET160 3.9 47.1 1.0 O B:GLN151 4.1 36.0 1.0 NE2 B:HIS114 4.1 27.7 1.0 CA B:HIS114 4.2 35.1 1.0 CB B:MET160 4.3 47.0 1.0 CD2 B:HIS114 4.4 25.6 1.0 ND1 B:HIS157 4.4 26.7 1.0 CA B:CYS153 4.5 32.0 1.0 O B:ILE113 4.6 36.6 1.0 CD1 B:PHE88 4.7 44.9 1.0 N B:CYS153 4.7 29.9 1.0 CA B:CYS149 4.8 41.4 1.0 O B:PHE86 4.8 45.0 1.0 N B:GLY115 4.9 40.7 1.0

T.Soulimane, G.Buse, G.P.Bourenkov, H.D.Bartunik, R.Huber, M.E.Than. Structure and Mechanism of the Aberrant Ba(3)-Cytochrome C Oxidase From Thermus Thermophilus. Embo J. V. 19 1766 2000.
ISSN: ISSN 0261-4189
PubMed: 10775261
DOI: 10.1093/EMBOJ/19.8.1766