Zinc in PDB 1e9q: Crystal Structure of Bovine Cu Zn Sod - (1 of 3)

All present enzymatic activity of Crystal Structure of Bovine Cu Zn Sod - (1 of 3):
1.13.1.1;

The structure of Crystal Structure of Bovine Cu Zn Sod - (1 of 3), PDB code: 1e9q 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)	25 / 1.75
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	47.600, 50.900, 147.600, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 20.5

The structure of Crystal Structure of Bovine Cu Zn Sod - (1 of 3) also contains other interesting chemical elements:

Copper

(Cu)

3 atoms

The binding sites of Zinc atom in the Crystal Structure of Bovine Cu Zn Sod - (1 of 3) (pdb code 1e9q). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Bovine Cu Zn Sod - (1 of 3), PDB code: 1e9q:

Zinc binding site 1 out of 1 in the Crystal Structure of Bovine Cu Zn Sod - (1 of 3)


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 Bovine Cu Zn Sod - (1 of 3) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn153 b:11.1 occ:1.00 OD1 B:ASP81 2.0 12.0 1.0 ND1 B:HIS78 2.0 9.0 1.0 ND1 B:HIS61 2.0 11.2 1.0 ND1 B:HIS69 2.1 7.6 1.0 CG B:ASP81 2.8 11.3 1.0 OD2 B:ASP81 2.9 11.2 1.0 CE1 B:HIS78 3.0 13.2 1.0 CE1 B:HIS61 3.0 13.0 1.0 CG B:HIS61 3.0 11.9 1.0 CG B:HIS78 3.0 11.0 1.0 CE1 B:HIS69 3.1 7.1 1.0 CG B:HIS69 3.2 9.3 1.0 CB B:HIS61 3.4 11.0 1.0 CB B:HIS78 3.5 9.3 1.0 CB B:HIS69 3.7 9.8 1.0 O B:SER134 3.7 14.8 1.0 O B:HOH2074 3.7 70.8 1.0 CA B:HIS69 4.0 10.8 1.0 NE2 B:HIS78 4.1 12.3 1.0 CD2 B:HIS78 4.1 11.4 1.0 NE2 B:HIS61 4.1 14.0 1.0 CD2 B:HIS61 4.2 12.9 1.0 NE2 B:HIS69 4.2 9.1 1.0 CB B:ASP81 4.2 11.9 1.0 CD2 B:HIS69 4.3 8.3 1.0 O B:HOH2037 4.4 70.4 1.0 O B:HOH2120 4.7 16.7 1.0 CA B:ASP81 4.7 12.2 1.0 N B:HIS78 4.7 10.5 1.0 C B:SER134 4.7 15.3 1.0 CA B:HIS78 4.8 9.9 1.0 N B:ASP81 4.8 11.1 1.0 N B:GLY70 4.9 11.8 1.0 N B:HIS69 4.9 10.4 1.0 C B:HIS69 5.0 12.2 1.0 CA B:HIS61 5.0 11.8 1.0

M.A.Hough, R.W.Strange, S.S.Hasnain. Conformational Variability of the Cu Site in One Subunit of Bovine Cuzn Superoxide Dismutase: the Importance of Mobility in the GLU119-LEU142 Loop Region For Catalytic Function J.Mol.Biol. V. 304 231 2000.
ISSN: ISSN 0022-2836
PubMed: 11080458
DOI: 10.1006/JMBI.2000.4186