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

The binding sites of Copper 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 Copper atom.
In total 2 binding sites of Copper where determined in the Monomeric Human Cu,Zn Superoxide Dismutase, Mutation H43F, PDB code: 4bcy:
Jump to Copper binding site number: 1; 2;

Copper 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 Copper with other atoms in the Cu 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:Cu1153 b:26.5 occ:0.47 CU A:CU1154 0.8 17.9 0.4 NE2 A:HIS48 2.0 22.0 1.0 ND1 A:HIS46 2.1 22.1 1.0 NE2 A:HIS120 2.1 22.3 1.0 NE2 A:HIS63 2.7 23.1 1.0 CE1 A:HIS48 2.8 24.6 1.0 O A:HOH2019 2.9 19.9 0.6 CE1 A:HIS46 3.0 21.9 1.0 CE1 A:HIS120 3.0 23.0 1.0 CG A:HIS46 3.0 18.8 1.0 CD2 A:HIS120 3.1 22.9 1.0 CD2 A:HIS48 3.2 21.0 1.0 CD2 A:HIS63 3.2 23.2 1.0 CB A:HIS46 3.4 20.3 1.0 CE1 A:HIS63 3.7 21.5 1.0 ND1 A:HIS48 4.0 24.3 1.0 NE2 A:HIS46 4.1 20.1 1.0 CD2 A:HIS46 4.1 19.4 1.0 ND1 A:HIS120 4.1 24.2 1.0 CG A:HIS48 4.2 21.3 1.0 CG A:HIS120 4.2 21.7 1.0 CG A:HIS63 4.2 21.0 1.0 ND1 A:HIS63 4.4 19.1 1.0 CA A:HIS46 4.6 18.3 1.0 CG1 A:VAL118 4.6 22.7 1.0 N A:HIS46 4.7 18.9 1.0 CB A:VAL118 4.8 19.8 1.0 O A:HOH2061 4.9 28.4 1.0

Copper 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 Copper with other atoms in the Cu 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:Cu1154 b:17.9 occ:0.44 CU A:CU1153 0.8 26.5 0.5 NE2 A:HIS48 1.9 22.0 1.0 NE2 A:HIS120 2.0 22.3 1.0 ND1 A:HIS46 2.1 22.1 1.0 CD2 A:HIS120 2.8 22.9 1.0 CD2 A:HIS48 2.9 21.0 1.0 CG A:HIS46 2.9 18.8 1.0 CE1 A:HIS48 3.0 24.6 1.0 CE1 A:HIS120 3.1 23.0 1.0 CB A:HIS46 3.1 20.3 1.0 CE1 A:HIS46 3.2 21.9 1.0 NE2 A:HIS63 3.5 23.1 1.0 O A:HOH2019 3.5 19.9 0.6 CD2 A:HIS63 3.8 23.2 1.0 CG1 A:VAL118 4.0 22.7 1.0 CG A:HIS120 4.0 21.7 1.0 CG A:HIS48 4.0 21.3 1.0 ND1 A:HIS48 4.0 24.3 1.0 CB A:VAL118 4.1 19.8 1.0 ND1 A:HIS120 4.1 24.2 1.0 N A:HIS46 4.1 18.9 1.0 CA A:HIS46 4.1 18.3 1.0 CD2 A:HIS46 4.1 19.4 1.0 NE2 A:HIS46 4.2 20.1 1.0 CE1 A:HIS63 4.3 21.5 1.0 O A:HIS46 4.5 19.0 1.0 O A:VAL118 4.6 21.2 1.0 C A:HIS46 4.6 17.1 1.0 CG A:HIS63 4.8 21.0 1.0 CG2 A:VAL118 4.9 21.9 1.0 C A:PHE45 4.9 19.5 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