Copper in PDB 1e9o: Crystal Structure of Bovine Sod - 1 of 3

All present enzymatic activity of Crystal Structure of Bovine Sod - 1 of 3:
1.15.1.1;

The structure of Crystal Structure of Bovine Sod - 1 of 3, PDB code: 1e9o 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)	8 / 1.85
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	47.500, 51.000, 147.800, 90.00, 90.00, 90.00
R / Rfree (%)	19.9 / 23

The binding sites of Copper atom in the Crystal Structure of Bovine Sod - 1 of 3 (pdb code 1e9o). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Crystal Structure of Bovine Sod - 1 of 3, PDB code: 1e9o:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in the Crystal Structure of Bovine Sod - 1 of 3


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 Bovine Sod - 1 of 3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu152 b:36.0 occ:1.00 NE2 A:HIS118 2.0 20.2 1.0 ND1 A:HIS44 2.1 22.4 1.0 NE2 A:HIS46 2.2 21.3 1.0 NE2 A:HIS61 2.5 27.5 1.0 CD2 A:HIS118 2.6 21.1 1.0 O A:HOH2076 3.0 54.9 1.0 CG A:HIS44 3.1 20.0 1.0 CE1 A:HIS44 3.1 20.7 1.0 CE1 A:HIS46 3.1 21.7 1.0 CD2 A:HIS61 3.2 22.7 1.0 CE1 A:HIS118 3.2 22.3 1.0 CB A:HIS44 3.3 19.4 1.0 CD2 A:HIS46 3.3 19.1 1.0 CE1 A:HIS61 3.7 24.4 1.0 CG A:HIS118 3.9 22.5 1.0 ND1 A:HIS118 4.1 23.3 1.0 NE2 A:HIS44 4.2 20.9 1.0 CD2 A:HIS44 4.3 21.0 1.0 ND1 A:HIS46 4.3 19.0 1.0 CG A:HIS46 4.4 18.3 1.0 CG A:HIS61 4.5 23.1 1.0 CG1 A:VAL116 4.5 20.8 1.0 CA A:HIS44 4.5 16.5 1.0 CB A:VAL116 4.5 20.0 1.0 N A:HIS44 4.5 15.7 1.0 O A:HOH2036 4.6 48.6 1.0 ND1 A:HIS61 4.7 23.1 1.0 O A:HOH2089 5.0 30.1 1.0

Copper binding site 2 out of 4 in the Crystal Structure of Bovine Sod - 1 of 3


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 Bovine Sod - 1 of 3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu153 b:20.4 occ:1.00 ND1 A:HIS69 2.0 20.3 1.0 OD1 A:ASP81 2.0 20.2 1.0 ND1 A:HIS78 2.0 18.9 1.0 ND1 A:HIS61 2.0 23.1 1.0 CG A:ASP81 2.8 19.9 1.0 CE1 A:HIS69 2.9 21.8 1.0 CE1 A:HIS78 2.9 18.1 1.0 CE1 A:HIS61 2.9 24.4 1.0 OD2 A:ASP81 3.0 19.6 1.0 CG A:HIS61 3.0 23.1 1.0 CG A:HIS78 3.1 17.9 1.0 CG A:HIS69 3.2 20.6 1.0 CB A:HIS61 3.5 21.7 1.0 CB A:HIS78 3.6 16.0 1.0 CB A:HIS69 3.6 20.8 1.0 O A:LYS134 3.9 26.3 1.0 CA A:HIS69 4.0 20.3 1.0 NE2 A:HIS78 4.0 17.9 1.0 NE2 A:HIS61 4.0 27.5 1.0 NE2 A:HIS69 4.1 20.6 1.0 CD2 A:HIS61 4.1 22.7 1.0 CD2 A:HIS78 4.1 17.5 1.0 CD2 A:HIS69 4.2 19.9 1.0 CB A:ASP81 4.2 19.1 1.0 CA A:ASP81 4.7 19.5 1.0 N A:HIS78 4.7 17.5 1.0 O A:HOH2087 4.7 38.5 1.0 CA A:HIS78 4.8 16.8 1.0 N A:ASP81 4.9 17.7 1.0 N A:GLY70 4.9 21.2 1.0 C A:LYS134 4.9 28.4 1.0 C A:HIS69 4.9 22.0 1.0 N A:HIS69 5.0 21.4 1.0 CA A:HIS61 5.0 22.0 1.0

Copper binding site 3 out of 4 in the Crystal Structure of Bovine Sod - 1 of 3


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 Bovine Sod - 1 of 3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu152 b:22.6 occ:1.00 NE2 B:HIS61 2.1 16.6 1.0 NE2 B:HIS46 2.1 17.1 1.0 NE2 B:HIS118 2.1 17.3 1.0 ND1 B:HIS44 2.2 16.9 1.0 O B:HOH2049 2.5 25.1 1.0 CE1 B:HIS46 2.8 15.7 1.0 CD2 B:HIS61 2.9 15.6 1.0 CE1 B:HIS118 3.0 13.5 1.0 CG B:HIS44 3.0 17.4 1.0 CE1 B:HIS61 3.1 16.6 1.0 CD2 B:HIS118 3.1 16.2 1.0 CE1 B:HIS44 3.2 18.1 1.0 CB B:HIS44 3.3 15.6 1.0 CD2 B:HIS46 3.3 14.0 1.0 ND1 B:HIS46 4.0 16.2 1.0 ND1 B:HIS118 4.1 16.8 1.0 CG B:HIS61 4.1 15.7 1.0 ND1 B:HIS61 4.1 13.7 1.0 CD2 B:HIS44 4.2 17.6 1.0 CG B:HIS118 4.2 15.7 1.0 NE2 B:HIS44 4.2 18.8 1.0 CG B:HIS46 4.2 14.1 1.0 CA B:HIS44 4.6 15.0 1.0 O B:HOH2036 4.7 88.7 1.0 N B:HIS44 4.8 14.6 1.0 CB B:VAL116 4.9 15.6 1.0 O B:HOH2124 4.9 20.4 1.0 CG1 B:VAL116 4.9 16.6 1.0

Copper binding site 4 out of 4 in the Crystal Structure of Bovine Sod - 1 of 3


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structure of Bovine Sod - 1 of 3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu153 b:15.7 occ:1.00 ND1 B:HIS78 1.9 12.5 1.0 OD1 B:ASP81 2.0 16.0 1.0 ND1 B:HIS61 2.0 13.7 1.0 ND1 B:HIS69 2.1 15.2 1.0 CG B:ASP81 2.8 14.7 1.0 CE1 B:HIS69 2.9 16.5 1.0 CE1 B:HIS78 2.9 15.4 1.0 OD2 B:ASP81 3.0 17.4 1.0 CG B:HIS78 3.0 12.8 1.0 CE1 B:HIS61 3.0 16.6 1.0 CG B:HIS61 3.0 15.7 1.0 CG B:HIS69 3.2 13.9 1.0 CB B:HIS61 3.4 13.2 1.0 CB B:HIS78 3.5 9.8 1.0 CB B:HIS69 3.7 13.6 1.0 O B:SER134 3.8 16.8 1.0 O B:HOH2072 3.9 86.0 1.0 CA B:HIS69 4.0 13.5 1.0 NE2 B:HIS78 4.0 15.0 1.0 CD2 B:HIS78 4.1 12.5 1.0 NE2 B:HIS69 4.1 15.9 1.0 NE2 B:HIS61 4.1 16.6 1.0 CD2 B:HIS61 4.2 15.6 1.0 CB B:ASP81 4.3 14.1 1.0 CD2 B:HIS69 4.3 14.0 1.0 O B:HOH2036 4.4 88.7 1.0 O B:HOH2121 4.7 17.9 1.0 CA B:ASP81 4.7 16.9 1.0 N B:HIS78 4.7 13.3 1.0 C B:SER134 4.7 17.3 1.0 CA B:HIS78 4.8 13.1 1.0 N B:GLY70 4.8 14.6 1.0 N B:ASP81 4.9 16.1 1.0 CA B:HIS61 5.0 14.7 1.0 C B:HIS69 5.0 16.4 1.0 N B:HIS69 5.0 14.4 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