Zinc in PDB 2gbt: C6A/C111A Cuzn Superoxide Dismutase

All present enzymatic activity of C6A/C111A Cuzn Superoxide Dismutase:
1.15.1.1;

The structure of C6A/C111A Cuzn Superoxide Dismutase, PDB code: 2gbt was solved by A.Hornberg, D.T.Logan, S.L.Marklund, M.Oliveberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.70
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	156.618, 35.257, 114.971, 90.00, 112.17, 90.00
R / Rfree (%)	20.3 / 23

The structure of C6A/C111A Cuzn Superoxide Dismutase also contains other interesting chemical elements:

Copper

(Cu)

2 atoms

The binding sites of Zinc atom in the C6A/C111A Cuzn Superoxide Dismutase (pdb code 2gbt). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the C6A/C111A Cuzn Superoxide Dismutase, PDB code: 2gbt:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the C6A/C111A Cuzn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of C6A/C111A Cuzn Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn155 b:38.9 occ:0.75 OD1 A:ASP83 1.8 36.0 1.0 ND1 A:HIS80 2.0 36.0 1.0 ND1 A:HIS63 2.1 39.9 1.0 ND1 A:HIS71 2.3 34.9 1.0 CG A:ASP83 2.7 35.8 1.0 CE1 A:HIS80 2.8 36.5 1.0 CE1 A:HIS63 2.9 40.5 1.0 OD2 A:ASP83 3.0 37.3 1.0 CG A:HIS80 3.0 36.4 1.0 CE1 A:HIS71 3.1 36.2 1.0 CG A:HIS63 3.2 39.2 1.0 CG A:HIS71 3.4 36.3 1.0 CB A:HIS80 3.6 35.7 1.0 CB A:HIS63 3.6 38.4 1.0 CB A:HIS71 3.8 36.1 1.0 NE2 A:HIS80 3.8 35.8 1.0 CD2 A:HIS80 4.0 36.1 1.0 NE2 A:HIS63 4.1 40.4 1.0 CB A:ASP83 4.1 36.1 1.0 CA A:HIS71 4.1 36.5 1.0 CD2 A:HIS63 4.2 40.5 1.0 O A:LYS136 4.3 39.0 1.0 NE2 A:HIS71 4.3 35.5 1.0 CD2 A:HIS71 4.5 35.2 1.0 CA A:ASP83 4.5 36.4 1.0 N A:HIS80 4.8 35.9 1.0 CA A:HIS80 4.8 35.9 1.0 N A:ASP83 4.8 36.2 1.0 O A:HOH225 4.9 44.4 1.0 N A:GLY72 5.0 36.2 1.0

Zinc binding site 2 out of 2 in the C6A/C111A Cuzn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of C6A/C111A Cuzn Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn155 b:38.5 occ:0.43 ND1 B:HIS63 1.9 37.9 1.0 OD1 B:ASP83 1.9 37.2 1.0 ND1 B:HIS71 2.3 38.2 1.0 ND1 B:HIS80 2.3 36.9 1.0 CE1 B:HIS63 2.7 38.1 1.0 CG B:ASP83 2.8 36.4 1.0 CE1 B:HIS80 3.0 36.1 1.0 CG B:HIS63 3.0 36.9 1.0 CE1 B:HIS71 3.0 38.7 1.0 OD2 B:ASP83 3.1 36.7 1.0 CG B:HIS80 3.3 36.8 1.0 CG B:HIS71 3.4 38.9 1.0 CB B:HIS63 3.5 36.6 1.0 CB B:HIS71 3.8 38.8 1.0 CB B:HIS80 3.8 36.6 1.0 NE2 B:HIS63 3.9 37.8 1.0 CD2 B:HIS63 4.1 37.7 1.0 NE2 B:HIS80 4.1 37.1 1.0 CB B:ASP83 4.2 36.1 1.0 NE2 B:HIS71 4.2 38.0 1.0 CD2 B:HIS80 4.2 36.9 1.0 CA B:HIS71 4.3 38.7 1.0 CD2 B:HIS71 4.4 38.1 1.0 O B:LYS136 4.4 42.5 1.0 CA B:ASP83 4.6 36.4 1.0 O B:HOH283 4.9 42.1 1.0 N B:ASP83 4.9 35.9 1.0 N B:GLY72 5.0 38.5 1.0 N B:HIS80 5.0 37.1 1.0 CD2 B:HIS46 5.0 37.6 1.0

A.Hornberg, D.T.Logan, S.L.Marklund, M.Oliveberg. The Coupling Between Disulphide Status, Metallation and Dimer Interface Strength in Cu/Zn Superoxide Dismutase J.Mol.Biol. V. 365 333 2007.
ISSN: ISSN 0022-2836
PubMed: 17070542
DOI: 10.1016/J.JMB.2006.09.048