Zinc in PDB 3hw7: High Pressure (0.57 Gpa) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase at 2.0 Angstroms

All present enzymatic activity of High Pressure (0.57 Gpa) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase at 2.0 Angstroms:
1.15.1.1;

The structure of High Pressure (0.57 Gpa) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase at 2.0 Angstroms, PDB code: 3hw7 was solved by I.Ascone, C.Savino, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.89 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.845, 50.509, 146.377, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 21.8

The structure of High Pressure (0.57 Gpa) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase at 2.0 Angstroms also contains other interesting chemical elements:

Copper

(Cu)

3 atoms

The binding sites of Zinc atom in the High Pressure (0.57 Gpa) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase at 2.0 Angstroms (pdb code 3hw7). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the High Pressure (0.57 Gpa) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase at 2.0 Angstroms, PDB code: 3hw7:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the High Pressure (0.57 Gpa) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase at 2.0 Angstroms


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of High Pressure (0.57 Gpa) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase at 2.0 Angstroms within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn153 b:16.4 occ:1.00 ND1 A:HIS78 2.0 12.9 1.0 OD2 A:ASP81 2.0 16.9 1.0 ND1 A:HIS69 2.0 19.2 1.0 ND1 A:HIS61 2.0 17.3 1.0 CG A:ASP81 2.7 16.5 1.0 OD1 A:ASP81 2.8 14.6 1.0 CE1 A:HIS78 2.8 17.2 1.0 CE1 A:HIS69 2.8 20.2 1.0 CG A:HIS61 3.0 16.7 1.0 CG A:HIS78 3.0 14.2 1.0 CE1 A:HIS61 3.1 17.1 1.0 CG A:HIS69 3.2 18.0 1.0 CB A:HIS61 3.3 16.1 1.0 CB A:HIS78 3.5 14.3 1.0 CB A:HIS69 3.7 18.1 1.0 O A:LYS134 3.9 25.1 1.0 NE2 A:HIS78 3.9 13.7 1.0 CA A:HIS69 4.0 19.0 1.0 NE2 A:HIS69 4.0 18.1 1.0 CD2 A:HIS78 4.1 12.8 1.0 CD2 A:HIS61 4.2 16.1 1.0 NE2 A:HIS61 4.2 16.1 1.0 CB A:ASP81 4.2 15.8 1.0 CD2 A:HIS69 4.2 17.5 1.0 O A:HOH253 4.6 19.1 1.0 N A:HIS78 4.6 16.1 1.0 CA A:HIS78 4.7 15.0 1.0 N A:GLY70 4.7 19.8 1.0 CA A:ASP81 4.7 16.5 1.0 CD2 A:HIS44 4.7 11.9 1.0 CA A:HIS61 4.8 15.6 1.0 C A:HIS69 4.9 19.6 1.0 C A:LYS134 4.9 25.9 1.0 N A:HIS69 5.0 19.0 1.0 O A:GLY70 5.0 21.4 1.0

Zinc binding site 2 out of 2 in the High Pressure (0.57 Gpa) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase at 2.0 Angstroms


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of High Pressure (0.57 Gpa) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase at 2.0 Angstroms within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn154 b:11.1 occ:1.00 ND1 B:HIS61 2.0 13.4 1.0 ND1 B:HIS69 2.0 10.6 1.0 OD1 B:ASP81 2.0 12.6 1.0 ND1 B:HIS78 2.1 10.1 1.0 CG B:ASP81 2.8 10.4 1.0 CE1 B:HIS69 2.8 12.5 1.0 OD2 B:ASP81 2.9 11.0 1.0 CE1 B:HIS61 2.9 15.8 1.0 CE1 B:HIS78 3.0 10.3 1.0 CG B:HIS61 3.0 11.5 1.0 CG B:HIS78 3.1 10.3 1.0 CG B:HIS69 3.1 10.4 1.0 CB B:HIS61 3.5 11.3 1.0 CB B:HIS78 3.5 9.4 1.0 CB B:HIS69 3.6 12.3 1.0 O B:LYS134 3.7 14.8 1.0 CA B:HIS69 3.9 11.8 1.0 NE2 B:HIS69 4.0 12.0 1.0 NE2 B:HIS61 4.0 15.6 1.0 NE2 B:HIS78 4.1 8.1 1.0 CD2 B:HIS61 4.1 13.9 1.0 CD2 B:HIS69 4.2 9.6 1.0 CB B:ASP81 4.2 11.4 1.0 CD2 B:HIS78 4.2 8.4 1.0 O B:HOH252 4.6 11.9 1.0 C B:LYS134 4.6 15.1 1.0 N B:HIS78 4.7 11.0 1.0 CA B:ASP81 4.7 11.9 1.0 N B:GLY70 4.7 11.9 1.0 CA B:HIS78 4.7 10.3 1.0 C B:HIS69 4.8 12.3 1.0 N B:HIS69 4.9 12.1 1.0 N B:ASP81 4.9 11.6 1.0 CA B:THR135 4.9 13.5 1.0 CA B:HIS61 5.0 11.9 1.0

I.Ascone, C.Savino, R.Kahn, R.Fourme. Flexibility of the Cu,Zn Superoxide Dismutase Structure Investigated at 0.57 Gpa Acta Crystallogr.,Sect.D V. 66 654 2010.
ISSN: ISSN 0907-4449
PubMed: 20516618
DOI: 10.1107/S0907444910012321