Copper in PDB 2zow: Crystal Structure of H2O2 Treated Cu,Zn-Sod

All present enzymatic activity of Crystal Structure of H2O2 Treated Cu,Zn-Sod:
1.15.1.1;

The structure of Crystal Structure of H2O2 Treated Cu,Zn-Sod, PDB code: 2zow was solved by S.Ito, T.Ishii, H.Sakai, K.Uchida, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.94 / 1.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.631, 51.009, 146.990, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 22.1

The binding sites of Copper atom in the Crystal Structure of H2O2 Treated Cu,Zn-Sod (pdb code 2zow). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of H2O2 Treated Cu,Zn-Sod, PDB code: 2zow:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Crystal Structure of H2O2 Treated Cu,Zn-Sod


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 H2O2 Treated Cu,Zn-Sod within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu301 b:17.6 occ:1.00 NE2 A:HIS46 2.0 13.3 1.0 NE2 A:HIS118 2.0 14.5 1.0 ND1 A:HIS44 2.0 14.5 1.0 CD2 A:HIS118 2.9 13.7 1.0 CE1 A:HIS46 3.0 12.0 1.0 CG A:HIS44 3.0 14.1 1.0 CD2 A:HIS46 3.0 12.9 1.0 CE1 A:HIS44 3.0 15.7 1.0 CE1 A:HIS118 3.1 15.0 1.0 NE2 A:HIS61 3.2 16.7 1.0 CB A:HIS44 3.3 13.7 1.0 CD2 A:HIS61 3.6 14.7 1.0 O A:HOH466 3.7 32.5 1.0 O A:HOH401 3.8 26.4 1.0 CB A:VAL116 4.0 14.4 1.0 ND1 A:HIS46 4.1 12.1 1.0 CG A:HIS118 4.1 13.7 1.0 ND1 A:HIS118 4.1 15.2 1.0 NE2 A:HIS44 4.1 16.2 1.0 CD2 A:HIS44 4.1 17.1 1.0 CG A:HIS46 4.1 12.1 1.0 N A:HIS44 4.1 12.1 1.0 CG1 A:VAL116 4.1 15.7 1.0 CE1 A:HIS61 4.1 15.6 1.0 CA A:HIS44 4.2 13.0 1.0 O A:VAL116 4.4 14.1 1.0 O A:HIS44 4.5 13.5 1.0 CG A:HIS61 4.6 15.6 1.0 C A:HIS44 4.6 11.9 1.0 CG2 A:VAL116 4.8 15.4 1.0 ND1 A:HIS61 4.9 14.0 1.0 C A:VAL116 4.9 13.0 1.0

Copper binding site 2 out of 2 in the Crystal Structure of H2O2 Treated Cu,Zn-Sod


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 H2O2 Treated Cu,Zn-Sod within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu301 b:15.4 occ:1.00 NE2 B:HIS46 2.0 11.1 1.0 ND1 B:HIS44 2.0 13.5 1.0 NE2 B:HIS118 2.1 10.3 1.0 CD2 B:HIS118 2.9 10.8 1.0 CE1 B:HIS46 3.0 12.4 1.0 CG B:HIS44 3.0 10.8 1.0 CD2 B:HIS46 3.0 10.7 1.0 CE1 B:HIS44 3.0 12.6 1.0 CE1 B:HIS118 3.1 11.1 1.0 NE2 B:HIS61 3.2 10.8 1.0 CB B:HIS44 3.3 10.7 1.0 O B:HOH433 3.5 17.3 1.0 CD2 B:HIS61 3.6 13.0 1.0 CB B:VAL116 3.9 9.8 1.0 ND1 B:HIS46 4.1 13.2 1.0 NE2 B:HIS44 4.1 10.5 1.0 CD2 B:HIS44 4.1 11.5 1.0 CG B:HIS118 4.1 10.9 1.0 CG B:HIS46 4.1 11.1 1.0 CE1 B:HIS61 4.1 11.4 1.0 N B:HIS44 4.2 10.2 1.0 CG1 B:VAL116 4.2 12.5 1.0 ND1 B:HIS118 4.2 11.8 1.0 CA B:HIS44 4.2 10.3 1.0 O B:VAL116 4.4 11.7 1.0 O B:HIS44 4.5 10.4 1.0 C B:HIS44 4.6 9.2 1.0 CG B:HIS61 4.6 12.3 1.0 CG2 B:VAL116 4.7 12.6 1.0 ND1 B:HIS61 4.9 12.5 1.0 C B:VAL116 4.9 10.5 1.0 CA B:VAL116 5.0 10.2 1.0

S.Ito, T.Ishii, H.Sakai, K.Uchida. Crystal Structures of H2O2-Treated Cu,Zn-Superoxide Dismutase To Be Published.