Copper 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:

Zinc

(Zn)

1 atom

The binding sites of Copper 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 Copper atom.
In total 3 binding sites of Copper where determined in the Crystal Structure of Bovine Cu Zn Sod - (1 of 3), PDB code: 1e9q:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in the Crystal Structure of Bovine Cu Zn 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 Cu Zn Sod - (1 of 3) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu152 b:27.7 occ:1.00 NE2 A:HIS61 2.1 17.2 1.0 ND1 A:HIS44 2.1 16.1 1.0 NE2 A:HIS118 2.2 14.1 1.0 NE2 A:HIS46 2.3 10.5 1.0 CE1 A:HIS118 2.5 15.8 1.0 CD2 A:HIS61 2.7 17.5 1.0 CG A:HIS44 2.9 14.2 1.0 O A:HOH2092 3.0 29.3 1.0 CE1 A:HIS44 3.0 15.0 1.0 CE1 A:HIS46 3.2 12.1 1.0 CB A:HIS44 3.2 13.9 1.0 CE1 A:HIS61 3.3 18.4 1.0 CD2 A:HIS46 3.3 12.5 1.0 CD2 A:HIS118 3.5 16.3 1.0 ND1 A:HIS118 3.7 15.4 1.0 CG A:HIS61 4.0 16.5 1.0 CD2 A:HIS44 4.1 15.9 1.0 NE2 A:HIS44 4.1 15.5 1.0 ND1 A:HIS61 4.2 16.5 1.0 CG A:HIS118 4.2 14.7 1.0 ND1 A:HIS46 4.3 12.0 1.0 CG A:HIS46 4.4 10.8 1.0 CA A:HIS44 4.5 13.4 1.0 N A:HIS44 4.6 12.6 1.0 CB A:VAL116 4.8 13.4 1.0 O A:HOH2036 4.9 29.5 1.0 CG1 A:VAL116 4.9 13.9 1.0

Copper binding site 2 out of 3 in the Crystal Structure of Bovine Cu Zn 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 Cu Zn Sod - (1 of 3) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu153 b:14.7 occ:1.00 ND1 A:HIS78 2.0 13.1 1.0 OD1 A:ASP81 2.1 14.1 1.0 ND1 A:HIS69 2.1 16.5 1.0 ND1 A:HIS61 2.3 16.5 1.0 CG A:ASP81 2.8 16.6 1.0 OD2 A:ASP81 2.8 15.0 1.0 CE1 A:HIS78 2.9 14.0 1.0 CE1 A:HIS69 2.9 16.7 1.0 CG A:HIS78 3.1 13.2 1.0 CG A:HIS61 3.1 16.5 1.0 CE1 A:HIS61 3.2 18.4 1.0 CG A:HIS69 3.2 17.2 1.0 CB A:HIS61 3.5 15.5 1.0 CB A:HIS78 3.5 13.0 1.0 CB A:HIS69 3.6 17.0 1.0 O A:LYS134 3.9 24.8 1.0 CA A:HIS69 4.0 16.8 1.0 NE2 A:HIS78 4.0 13.9 1.0 NE2 A:HIS69 4.1 16.8 1.0 CD2 A:HIS78 4.1 12.7 1.0 NE2 A:HIS61 4.2 17.2 1.0 CD2 A:HIS61 4.2 17.5 1.0 CB A:ASP81 4.2 14.7 1.0 CD2 A:HIS69 4.2 16.6 1.0 O A:HOH2090 4.6 20.8 1.0 N A:HIS78 4.7 14.6 1.0 CA A:ASP81 4.7 14.5 1.0 CA A:HIS78 4.7 13.6 1.0 N A:GLY70 4.9 17.7 1.0 N A:ASP81 4.9 13.6 1.0 C A:LYS134 4.9 24.8 1.0 C A:HIS69 4.9 18.0 1.0 N A:HIS69 5.0 17.6 1.0 CD2 A:HIS44 5.0 15.9 1.0 CA A:HIS61 5.0 14.1 1.0

Copper binding site 3 out of 3 in the Crystal Structure of Bovine Cu Zn 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 Cu Zn Sod - (1 of 3) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu152 b:20.7 occ:1.00 NE2 B:HIS61 2.1 14.0 1.0 ND1 B:HIS44 2.1 12.4 1.0 NE2 B:HIS118 2.2 10.0 1.0 NE2 B:HIS46 2.2 11.9 1.0 O B:HOH2050 2.6 23.9 1.0 CE1 B:HIS46 2.9 12.9 1.0 CE1 B:HIS118 2.9 12.1 1.0 CD2 B:HIS61 2.9 12.9 1.0 CG B:HIS44 3.0 11.8 1.0 CE1 B:HIS44 3.1 12.3 1.0 CD2 B:HIS118 3.1 10.4 1.0 CE1 B:HIS61 3.2 13.0 1.0 CB B:HIS44 3.3 12.2 1.0 CD2 B:HIS46 3.3 12.4 1.0 ND1 B:HIS46 4.1 12.3 1.0 ND1 B:HIS118 4.1 10.6 1.0 CD2 B:HIS44 4.1 11.7 1.0 CG B:HIS61 4.2 11.9 1.0 CG B:HIS118 4.2 11.3 1.0 NE2 B:HIS44 4.2 11.5 1.0 ND1 B:HIS61 4.2 11.2 1.0 CG B:HIS46 4.3 11.8 1.0 CA B:HIS44 4.6 10.2 1.0 O B:HOH2037 4.8 70.4 1.0 CB B:VAL116 4.8 11.5 1.0 O B:HOH2122 4.8 19.6 1.0 N B:HIS44 4.8 11.7 1.0 CG1 B:VAL116 4.9 13.5 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