Zinc in PDB 4ff9: Crystal Structure of Cysteinylated Wt SOD1.

All present enzymatic activity of Crystal Structure of Cysteinylated Wt SOD1.:
1.15.1.1;

The structure of Crystal Structure of Cysteinylated Wt SOD1., PDB code: 4ff9 was solved by J.R.Auclair, H.R.Brodkin, J.A.D'aquino, D.Ringe, G.A.Petsko, J.N.Agar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.15 / 2.50
Space group	P 63
Cell size a, b, c (Å), α, β, γ (°)	113.050, 113.050, 70.590, 90.00, 90.00, 120.00
R / Rfree (%)	27.6 / 33.5

The structure of Crystal Structure of Cysteinylated Wt SOD1. also contains other interesting chemical elements:

Copper

(Cu)

2 atoms

The binding sites of Zinc atom in the Crystal Structure of Cysteinylated Wt SOD1. (pdb code 4ff9). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Cysteinylated Wt SOD1., PDB code: 4ff9:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Cysteinylated Wt SOD1.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Cysteinylated Wt SOD1. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn202 b:31.0 occ:1.00 ND1 A:HIS63 2.0 35.4 1.0 OD2 A:ASP83 2.0 40.8 1.0 ND1 A:HIS80 2.1 39.6 1.0 ND1 A:HIS71 2.2 19.8 1.0 CG A:ASP83 2.8 36.8 1.0 CE1 A:HIS63 3.0 27.1 1.0 OD1 A:ASP83 3.0 34.9 1.0 CG A:HIS80 3.0 34.2 1.0 CG A:HIS63 3.1 33.4 1.0 CE1 A:HIS71 3.1 17.9 1.0 CE1 A:HIS80 3.1 38.8 1.0 CB A:HIS80 3.3 31.0 1.0 CG A:HIS71 3.3 25.8 1.0 CB A:HIS63 3.4 29.4 1.0 CB A:HIS71 3.8 28.1 1.0 O A:LYS136 3.9 27.8 1.0 CA A:HIS71 4.1 20.9 1.0 NE2 A:HIS63 4.1 34.0 1.0 CD2 A:HIS80 4.2 36.0 1.0 CD2 A:HIS63 4.2 33.4 1.0 NE2 A:HIS80 4.2 40.3 1.0 NE2 A:HIS71 4.2 21.3 1.0 CB A:ASP83 4.3 30.6 1.0 CD2 A:HIS71 4.4 22.0 1.0 CA A:HIS80 4.7 45.3 1.0 CA A:ASP83 4.7 25.2 1.0 CD2 A:HIS46 4.7 29.5 1.0 N A:GLY72 4.8 14.0 1.0 N A:HIS80 4.8 48.4 1.0 C A:LYS136 4.9 31.1 1.0 N A:ASP83 4.9 27.9 1.0 CA A:HIS63 4.9 29.1 1.0 O A:HOH308 5.0 33.4 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Cysteinylated Wt SOD1.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Cysteinylated Wt SOD1. within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:58.7 occ:1.00 ND1 B:HIS80 2.0 60.0 1.0 ND1 B:HIS63 2.2 56.0 1.0 OD1 B:ASP83 2.2 65.2 1.0 ND1 B:HIS71 2.3 47.7 1.0 CG B:HIS80 2.9 60.1 1.0 CE1 B:HIS80 2.9 63.3 1.0 CG B:ASP83 3.1 65.5 1.0 CG B:HIS63 3.1 57.0 1.0 CE1 B:HIS63 3.1 54.1 1.0 CE1 B:HIS71 3.2 54.3 1.0 CG B:HIS71 3.3 48.1 1.0 CB B:HIS80 3.3 57.8 1.0 OD2 B:ASP83 3.3 62.7 1.0 CB B:HIS63 3.3 58.9 1.0 O B:LYS136 3.5 70.0 1.0 CB B:HIS71 3.6 47.6 1.0 CA B:HIS71 3.9 57.9 1.0 NE2 B:HIS80 4.0 65.1 1.0 CD2 B:HIS80 4.0 63.8 1.0 CD2 B:HIS63 4.2 56.8 1.0 NE2 B:HIS63 4.2 54.5 1.0 NE2 B:HIS71 4.3 54.9 1.0 CB B:ASP83 4.4 67.2 1.0 CD2 B:HIS71 4.4 48.9 1.0 N B:GLY72 4.4 64.7 1.0 CA B:HIS80 4.6 60.6 1.0 N B:HIS80 4.6 66.4 1.0 C B:LYS136 4.7 70.8 1.0 C B:HIS71 4.7 61.9 1.0 NE2 B:HIS46 4.8 73.8 1.0 CE1 B:HIS46 4.8 70.5 1.0 CA B:ASP83 4.9 64.6 1.0 CA B:HIS63 4.9 56.8 1.0 N B:HIS71 4.9 57.8 1.0

J.R.Auclair, H.R.Brodkin, J.A.D'aquino, G.A.Petsko, D.Ringe, J.N.Agar. Structural Consequences of Cysteinylation of Cu/Zn-Superoxide Dismutase. Biochemistry V. 52 6145 2013.
ISSN: ISSN 0006-2960
PubMed: 23919400
DOI: 10.1021/BI400613H