Chlorine in PDB 4bcy: Monomeric Human Cu,Zn Superoxide Dismutase, Mutation H43F

All present enzymatic activity of Monomeric Human Cu,Zn Superoxide Dismutase, Mutation H43F:
1.15.1.1;

The structure of Monomeric Human Cu,Zn Superoxide Dismutase, Mutation H43F, PDB code: 4bcy was solved by W.Awad, K.Saraboji, J.Danielsson, L.Lang, M.Kurnik, S.L.Marklund, M.Oliveberg, D.T.Logan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.19 / 1.27
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	34.870, 47.910, 81.180, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 20.3

The structure of Monomeric Human Cu,Zn Superoxide Dismutase, Mutation H43F also contains other interesting chemical elements:

Cadmium	(Cd)	6 atoms
Copper	(Cu)	2 atoms
Zinc	(Zn)	1 atom

The binding sites of Chlorine atom in the Monomeric Human Cu,Zn Superoxide Dismutase, Mutation H43F (pdb code 4bcy). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Monomeric Human Cu,Zn Superoxide Dismutase, Mutation H43F, PDB code: 4bcy:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Monomeric Human Cu,Zn Superoxide Dismutase, Mutation H43F


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Monomeric Human Cu,Zn Superoxide Dismutase, Mutation H43F within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1162 b:52.7 occ:0.70 NZ A:LYS122 2.6 43.5 1.0 CE A:LYS122 3.4 43.1 1.0 CG A:LYS122 3.4 36.9 1.0 CD A:LYS122 3.9 41.3 1.0 CD A:GLU121 4.0 39.4 1.0 OE1 A:GLU121 4.0 43.8 1.0 OE2 A:GLU121 4.1 34.1 1.0 CG A:GLU121 4.7 34.9 1.0 CB A:LYS122 4.7 30.7 1.0

Chlorine binding site 2 out of 2 in the Monomeric Human Cu,Zn Superoxide Dismutase, Mutation H43F


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Monomeric Human Cu,Zn Superoxide Dismutase, Mutation H43F within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1163 b:54.5 occ:0.86 NH2 A:ARG143 2.4 22.9 0.5 CB A:GLU50 3.2 28.7 1.0 CA A:GLY61 3.3 36.4 1.0 O A:GLY61 3.3 29.9 1.0 N A:GLY61 3.4 39.5 1.0 N A:GLU50 3.4 25.0 1.0 C A:GLY61 3.4 32.4 1.0 CB A:HIS48 3.4 21.6 1.0 CZ A:ARG143 3.4 25.5 0.5 NH1 A:ARG143 3.6 23.8 0.5 CA A:GLU50 3.8 26.0 1.0 ND1 A:HIS48 3.9 24.3 1.0 N A:GLU49 4.0 24.1 1.0 CG A:HIS48 4.1 21.3 1.0 O A:PRO62 4.1 22.7 1.0 CG A:GLU50 4.3 29.0 0.6 N A:PRO62 4.3 27.0 1.0 C A:HIS48 4.4 20.9 1.0 C A:GLU49 4.5 25.5 1.0 OE1 A:GLU50 4.5 28.0 0.4 CA A:HIS48 4.5 18.5 1.0 C A:ALA60 4.5 39.6 0.7 NH2 A:ARG143 4.5 32.9 0.6 CA A:GLU49 4.6 25.7 1.0 NE A:ARG143 4.7 30.2 0.5 CB A:GLU49 4.9 30.4 1.0 N A:ALA60 4.9 35.8 0.7 CD A:GLU50 4.9 27.7 0.6 NE A:ARG143 4.9 33.2 0.6 C A:PRO62 5.0 21.8 1.0

J.Danielsson, W.Awad, K.Saraboji, M.Kurnik, L.Lang, L.Leinartaite, S.L.Marklund, D.T.Logan, M.Oliveberg. Global Structural Motions From the Strain of A Single Hydrogen Bond. Proc.Natl.Acad.Sci.Usa V. 110 3829 2013.
ISSN: ISSN 0027-8424
PubMed: 23431167
DOI: 10.1073/PNAS.1217306110