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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 7fb6:

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

Zinc (Zn) 2 atoms
Copper (Cu) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine 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 Chlorine atom.
In total only one binding site of Chlorine was determined in the C57D/C146D Mutant of Human Cu, Zn Superoxide Dismutase (SOD1), PDB code: 7fb6:

Chlorine binding site 1 out of 1 in 7fb6

Go back to Chlorine Binding Sites List in 7fb6
Chlorine binding site 1 out of 1 in the C57D/C146D Mutant of Human Cu, Zn Superoxide Dismutase (SOD1)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl 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:Cl156

b:27.8
occ:1.00
CG A:LYS75 3.2 27.8 1.0
CB A:LYS75 3.8 20.1 1.0
CD A:LYS75 4.4 23.7 1.0
CE A:LYS75 4.9 39.7 1.0

Reference:

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
Page generated: Mon Jul 29 20:43:57 2024

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