Zinc in PDB 1sxc: Crystal Structure of Reduced Bovine Erythrocyte Superoxide Dismutase at 1.9 Angstroms Resolution

All present enzymatic activity of Crystal Structure of Reduced Bovine Erythrocyte Superoxide Dismutase at 1.9 Angstroms Resolution:
1.15.1.1;

The structure of Crystal Structure of Reduced Bovine Erythrocyte Superoxide Dismutase at 1.9 Angstroms Resolution, PDB code: 1sxc was solved by W.R.Rypniewski, S.Mangani, B.Bruni, P.Orioli, M.Casati, K.S.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	47.800, 51.060, 147.990, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The structure of Crystal Structure of Reduced Bovine Erythrocyte Superoxide Dismutase at 1.9 Angstroms Resolution also contains other interesting chemical elements:

Copper

(Cu)

2 atoms

The binding sites of Zinc atom in the Crystal Structure of Reduced Bovine Erythrocyte Superoxide Dismutase at 1.9 Angstroms Resolution (pdb code 1sxc). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Reduced Bovine Erythrocyte Superoxide Dismutase at 1.9 Angstroms Resolution, PDB code: 1sxc:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Reduced Bovine Erythrocyte Superoxide Dismutase at 1.9 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Reduced Bovine Erythrocyte Superoxide Dismutase at 1.9 Angstroms Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn153 b:11.3 occ:1.00 OD1 A:ASP81 1.9 10.4 1.0 ND1 A:HIS61 2.0 11.7 1.0 ND1 A:HIS78 2.2 10.2 1.0 ND1 A:HIS69 2.2 13.4 1.0 CG A:ASP81 2.8 15.6 1.0 CE1 A:HIS61 3.0 13.4 1.0 CG A:HIS61 3.0 13.5 1.0 CE1 A:HIS78 3.0 11.4 1.0 CE1 A:HIS69 3.0 14.7 1.0 OD2 A:ASP81 3.1 10.5 1.0 CG A:HIS78 3.2 9.9 1.0 CG A:HIS69 3.3 15.2 1.0 CB A:HIS61 3.4 11.9 1.0 CB A:HIS78 3.6 7.0 1.0 CB A:HIS69 3.7 9.1 1.0 O A:LYS134 3.8 12.8 1.0 CA A:HIS69 4.0 11.9 1.0 NE2 A:HIS61 4.1 17.7 1.0 CD2 A:HIS61 4.1 14.0 1.0 NE2 A:HIS78 4.1 10.4 1.0 NE2 A:HIS69 4.2 12.5 1.0 CB A:ASP81 4.2 8.7 1.0 CD2 A:HIS78 4.3 8.7 1.0 CD2 A:HIS69 4.4 14.2 1.0 O A:HOH160 4.6 15.1 1.0 CA A:ASP81 4.7 10.6 1.0 N A:HIS78 4.7 10.8 1.0 CA A:HIS78 4.8 10.5 1.0 C A:LYS134 4.9 16.7 1.0 N A:ASP81 4.9 10.7 1.0 CA A:HIS61 4.9 8.1 1.0 N A:GLY70 4.9 12.1 1.0 C A:HIS69 4.9 16.3 1.0 N A:HIS69 5.0 12.6 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Reduced Bovine Erythrocyte Superoxide Dismutase at 1.9 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Reduced Bovine Erythrocyte Superoxide Dismutase at 1.9 Angstroms Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn153 b:9.1 occ:1.00 ND1 B:HIS78 1.9 5.3 1.0 OD1 B:ASP81 2.0 9.8 1.0 ND1 B:HIS61 2.1 10.0 1.0 ND1 B:HIS69 2.2 5.2 1.0 CG B:ASP81 2.8 6.3 1.0 OD2 B:ASP81 2.9 9.4 1.0 CE1 B:HIS78 3.0 9.3 1.0 CG B:HIS78 3.0 5.8 1.0 CE1 B:HIS61 3.0 10.6 1.0 CE1 B:HIS69 3.1 8.0 1.0 CG B:HIS61 3.1 9.1 1.0 CG B:HIS69 3.3 7.3 1.0 CB B:HIS61 3.5 6.8 1.0 CB B:HIS78 3.5 7.1 1.0 CB B:HIS69 3.7 6.7 1.0 O B:LYS134 3.7 11.3 1.0 CA B:HIS69 4.0 6.2 1.0 NE2 B:HIS78 4.1 8.4 1.0 CD2 B:HIS78 4.1 8.2 1.0 NE2 B:HIS61 4.2 10.5 1.0 CD2 B:HIS61 4.2 9.9 1.0 NE2 B:HIS69 4.2 6.9 1.0 CB B:ASP81 4.2 8.1 1.0 CD2 B:HIS69 4.3 4.9 1.0 CA B:ASP81 4.7 8.7 1.0 N B:HIS78 4.7 7.0 1.0 C B:LYS134 4.7 11.9 1.0 O B:HOH163 4.7 13.2 1.0 N B:ASP81 4.8 9.7 1.0 CA B:HIS78 4.8 5.6 1.0 N B:HIS69 4.9 8.2 1.0 N B:GLY70 4.9 7.9 1.0 C B:HIS69 5.0 10.0 1.0 CA B:HIS61 5.0 8.8 1.0 CA B:THR135 5.0 7.7 1.0

W.R.Rypniewski, S.Mangani, B.Bruni, P.L.Orioli, M.Casati, K.S.Wilson. Crystal Structure of Reduced Bovine Erythrocyte Superoxide Dismutase at 1.9 A Resolution. J.Mol.Biol. V. 251 282 1995.
ISSN: ISSN 0022-2836
PubMed: 7643403
DOI: 10.1006/JMBI.1995.0434