Copper in PDB 7fb6: C57D/C146D Mutant of Human Cu, Zn Superoxide Dismutase (SOD1)

All present enzymatic activity of C57D/C146D Mutant of Human Cu, Zn Superoxide Dismutase (SOD1):
1.15.1.1;

The structure of C57D/C146D Mutant of Human Cu, Zn Superoxide Dismutase (SOD1), PDB code: 7fb6 was solved by Y.Baek, N.-C.Ha, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.38 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.319, 48.554, 55.015, 90, 93.17, 90
R / Rfree (%)	18.4 / 21.3

The structure of C57D/C146D Mutant of Human Cu, Zn Superoxide Dismutase (SOD1) also contains other interesting chemical elements:

Zinc	(Zn)	2 atoms
Chlorine	(Cl)	1 atom

The binding sites of Copper atom in the C57D/C146D Mutant of Human Cu, Zn Superoxide Dismutase (SOD1) (pdb code 7fb6). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the C57D/C146D Mutant of Human Cu, Zn Superoxide Dismutase (SOD1), PDB code: 7fb6:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the C57D/C146D Mutant of Human Cu, Zn Superoxide Dismutase (SOD1)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of C57D/C146D Mutant of Human Cu, Zn Superoxide Dismutase (SOD1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu155 b:39.7 occ:1.00 NE2 A:HIS120 2.0 21.3 1.0 NE2 A:HIS48 2.2 18.3 1.0 ND1 A:HIS46 2.4 16.6 1.0 CE1 A:HIS120 2.8 19.9 1.0 NE2 A:HIS63 3.0 17.6 1.0 CE1 A:HIS48 3.0 29.0 1.0 CD2 A:HIS120 3.1 16.1 1.0 CG A:HIS46 3.2 17.4 1.0 CB A:HIS46 3.3 14.4 1.0 CD2 A:HIS48 3.3 16.9 1.0 CE1 A:HIS46 3.5 14.4 1.0 CD2 A:HIS63 3.5 19.1 1.0 ND1 A:HIS120 3.9 18.8 1.0 CE1 A:HIS63 4.0 15.5 1.0 CG A:HIS120 4.1 14.0 1.0 ND1 A:HIS48 4.2 22.6 1.0 NH1 A:ARG143 4.2 35.8 1.0 CG A:HIS48 4.4 19.0 1.0 CD2 A:HIS46 4.4 13.8 1.0 CB A:VAL118 4.5 12.6 1.0 NE2 A:HIS46 4.5 14.9 1.0 CG1 A:VAL118 4.5 15.3 1.0 CA A:HIS46 4.6 12.2 1.0 CG A:HIS63 4.6 16.8 1.0 ND1 A:HIS63 4.9 19.0 1.0 N A:HIS46 4.9 9.9 1.0 O A:HOH211 4.9 26.3 1.0

Copper binding site 2 out of 2 in the C57D/C146D Mutant of Human Cu, Zn Superoxide Dismutase (SOD1)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of C57D/C146D Mutant of Human Cu, Zn Superoxide Dismutase (SOD1) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu155 b:40.0 occ:1.00 NE2 B:HIS120 2.1 18.8 1.0 NE2 B:HIS48 2.2 15.3 1.0 ND1 B:HIS46 2.3 15.4 1.0 NE2 B:HIS63 2.5 12.0 1.0 CE1 B:HIS48 2.9 13.0 1.0 CG B:HIS46 3.0 14.2 1.0 CD2 B:HIS120 3.0 16.2 1.0 CE1 B:HIS120 3.0 18.0 1.0 CB B:HIS46 3.0 14.9 1.0 CD2 B:HIS63 3.2 15.0 1.0 CD2 B:HIS48 3.3 15.4 1.0 CE1 B:HIS46 3.4 16.0 1.0 CE1 B:HIS63 3.4 18.1 1.0 ND1 B:HIS120 4.0 16.4 1.0 CG B:HIS120 4.1 16.3 1.0 ND1 B:HIS48 4.1 16.4 1.0 CG B:HIS63 4.2 18.0 1.0 CD2 B:HIS46 4.2 12.3 1.0 ND1 B:HIS63 4.2 13.8 1.0 CG B:HIS48 4.3 14.3 1.0 NE2 B:HIS46 4.4 14.6 1.0 CA B:HIS46 4.4 12.8 1.0 O B:HOH175 4.7 19.5 1.0 N B:HIS46 4.8 12.8 1.0 CB B:VAL118 4.8 10.7 1.0 CG1 B:VAL118 4.8 17.0 1.0 C B:HIS46 5.0 12.0 1.0

Y.Baek, T.G.Woo, J.Ahn, D.Lee, Y.Kwon, B.J.Park, N.C.Ha. Structural Analysis of the Overoxidized Cu/Zn-Superoxide Dismutase in Ros-Induced Als Filament Formation. Commun Biol V. 5 1085 2022.
ISSN: ESSN 2399-3642
PubMed: 36224351
DOI: 10.1038/S42003-022-04017-0