Copper in PDB 1q0e: Atomic Resolution (1.15 ) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase

All present enzymatic activity of Atomic Resolution (1.15 ) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase:
1.15.1.1;

The structure of Atomic Resolution (1.15 ) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase, PDB code: 1q0e was solved by M.A.Hough, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.15
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.953, 51.507, 148.410, 90.00, 90.00, 90.00
R / Rfree (%)	13.1 / 16.6

The structure of Atomic Resolution (1.15 ) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Copper atom in the Atomic Resolution (1.15 ) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase (pdb code 1q0e). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Atomic Resolution (1.15 ) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase, PDB code: 1q0e:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in the Atomic Resolution (1.15 ) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Atomic Resolution (1.15 ) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu152 b:14.0 occ:1.00 NE2 A:HIS46 2.0 12.9 1.0 ND1 A:HIS44 2.0 13.5 1.0 NE2 A:HIS118 2.1 14.6 1.0 CE1 A:HIS46 2.9 12.7 1.0 CD2 A:HIS118 3.0 15.2 1.0 CD2 A:HIS46 3.0 12.1 1.0 CE1 A:HIS44 3.0 15.9 1.0 CG A:HIS44 3.1 13.4 1.0 CE1 A:HIS118 3.1 15.5 1.0 CB A:HIS44 3.4 13.1 1.0 NE2 A:HIS61 3.4 16.6 1.0 CD2 A:HIS61 3.6 18.0 1.0 CB A:VAL116 4.0 13.0 1.0 O A:HOH3071 4.0 24.8 1.0 ND1 A:HIS46 4.1 12.9 1.0 ND1 A:HIS118 4.2 16.0 1.0 CG A:HIS118 4.2 15.9 1.0 CG A:HIS46 4.2 11.6 1.0 NE2 A:HIS44 4.2 14.9 1.0 CG1 A:VAL116 4.2 14.6 1.0 N A:HIS44 4.2 12.3 1.0 CD2 A:HIS44 4.2 14.3 1.0 CA A:HIS44 4.3 11.6 1.0 O A:HOH3029 4.3 19.4 1.0 CE1 A:HIS61 4.4 14.3 1.0 O A:VAL116 4.4 14.1 1.0 O A:HIS44 4.5 11.9 1.0 C A:HIS44 4.7 11.3 1.0 CG A:HIS61 4.7 14.3 1.0 CG2 A:VAL116 4.8 13.8 1.0 C A:VAL116 4.9 12.7 1.0

Copper binding site 2 out of 3 in the Atomic Resolution (1.15 ) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Atomic Resolution (1.15 ) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu152 b:11.2 occ:0.10 CU B:CU152 0.0 11.2 0.1 CU B:CU152 1.4 10.2 0.9 ND1 B:HIS44 2.1 11.4 1.0 NE2 B:HIS61 2.1 12.3 1.0 NE2 B:HIS118 2.4 11.9 1.0 O B:HOH3207 2.6 23.2 1.0 CE1 B:HIS44 2.6 12.4 1.0 NE2 B:HIS46 2.7 10.5 1.0 O B:HOH3059 2.7 20.6 1.0 CD2 B:HIS61 2.9 12.6 1.0 CE1 B:HIS118 3.1 11.1 1.0 CE1 B:HIS61 3.1 11.1 1.0 CG B:HIS44 3.2 10.4 1.0 CE1 B:HIS46 3.2 10.5 1.0 CD2 B:HIS118 3.4 11.4 1.0 CB B:HIS44 3.8 11.6 1.0 NE2 B:HIS44 3.8 11.9 1.0 CD2 B:HIS46 3.9 10.2 1.0 CG B:HIS61 4.0 10.7 1.0 CD2 B:HIS44 4.0 11.8 1.0 ND1 B:HIS61 4.1 10.2 1.0 ND1 B:HIS118 4.2 10.7 1.0 CG B:HIS118 4.4 10.5 1.0 ND1 B:HIS46 4.4 10.9 1.0 O B:HOH3033 4.7 17.2 1.0 CG B:HIS46 4.8 10.0 1.0 O B:HOH3032 4.8 15.4 1.0 CA B:HIS44 5.0 10.3 1.0

Copper binding site 3 out of 3 in the Atomic Resolution (1.15 ) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Atomic Resolution (1.15 ) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu152 b:10.2 occ:0.90 CU B:CU152 0.0 10.2 0.9 CU B:CU152 1.4 11.2 0.1 NE2 B:HIS46 2.0 10.5 1.0 NE2 B:HIS118 2.0 11.9 1.0 ND1 B:HIS44 2.1 11.4 1.0 CE1 B:HIS46 3.0 10.5 1.0 CD2 B:HIS118 3.0 11.4 1.0 CE1 B:HIS44 3.0 12.4 1.0 CD2 B:HIS46 3.1 10.2 1.0 CG B:HIS44 3.1 10.4 1.0 CE1 B:HIS118 3.1 11.1 1.0 NE2 B:HIS61 3.3 12.3 1.0 CB B:HIS44 3.3 11.6 1.0 O B:HOH3059 3.7 20.6 1.0 CD2 B:HIS61 3.7 12.6 1.0 O B:HOH3207 3.7 23.2 1.0 CB B:VAL116 4.0 11.3 1.0 ND1 B:HIS46 4.1 10.9 1.0 CG1 B:VAL116 4.2 12.8 1.0 ND1 B:HIS118 4.2 10.7 1.0 CG B:HIS118 4.2 10.5 1.0 NE2 B:HIS44 4.2 11.9 1.0 CG B:HIS46 4.2 10.0 1.0 N B:HIS44 4.2 10.3 1.0 CD2 B:HIS44 4.2 11.8 1.0 CE1 B:HIS61 4.3 11.1 1.0 CA B:HIS44 4.3 10.3 1.0 O B:VAL116 4.4 11.4 1.0 O B:HIS44 4.5 10.7 1.0 C B:HIS44 4.7 10.3 1.0 CG2 B:VAL116 4.7 12.0 1.0 CG B:HIS61 4.8 10.7 1.0 C B:VAL116 5.0 10.5 1.0

M.A.Hough, S.S.Hasnain. Structure of Fully Reduced Bovine Copper Zinc Superoxide Dismutase at 1.15 A. Structure V. 11 937 2003.
ISSN: ISSN 0969-2126
PubMed: 12906825
DOI: 10.1016/S0969-2126(03)00155-2