Zinc in PDB 2aqs: Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91E, K94E Double Mutant

All present enzymatic activity of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91E, K94E Double Mutant:
1.15.1.1;

The structure of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91E, K94E Double Mutant, PDB code: 2aqs was solved by M.Didonato, C.J.Kassmann, C.K.Bruns, D.E.Cabelli, Z.Cao, L.B.Tabatabai, J.S.Kroll, E.D.Getzoff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.88 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	45.787, 66.492, 49.752, 90.00, 101.48, 90.00
R / Rfree (%)	18.5 / 20.3

The structure of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91E, K94E Double Mutant also contains other interesting chemical elements:

Copper

(Cu)

3 atoms

The binding sites of Zinc atom in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91E, K94E Double Mutant (pdb code 2aqs). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91E, K94E Double Mutant, PDB code: 2aqs:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91E, K94E Double Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91E, K94E Double Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:15.7 occ:1.00 OD1 A:ASP125 1.9 14.6 1.0 ND1 A:HIS104 2.0 13.8 1.0 ND1 A:HIS122 2.1 14.8 1.0 ND1 A:HIS113 2.1 17.4 1.0 CG A:ASP125 2.7 14.0 1.0 OD2 A:ASP125 2.8 15.6 1.0 CE1 A:HIS104 2.9 14.7 1.0 CE1 A:HIS113 3.0 16.6 1.0 CE1 A:HIS122 3.0 15.4 1.0 CG A:HIS122 3.1 15.8 1.0 CG A:HIS104 3.1 17.3 1.0 CG A:HIS113 3.2 15.0 1.0 CB A:HIS122 3.4 15.0 1.0 CB A:HIS104 3.5 17.0 1.0 CB A:HIS113 3.6 15.5 1.0 CA A:HIS113 3.8 15.5 1.0 NE2 A:HIS104 4.1 16.4 1.0 CB A:ASP125 4.1 14.0 1.0 NE2 A:HIS122 4.1 16.9 1.0 NE2 A:HIS113 4.2 15.2 1.0 CD2 A:HIS104 4.2 17.1 1.0 CD2 A:HIS122 4.2 17.1 1.0 CD2 A:HIS113 4.3 15.7 1.0 CD2 A:LEU173 4.5 16.9 1.0 CA A:ASP125 4.7 13.4 1.0 N A:GLY114 4.7 14.2 1.0 CA A:HIS122 4.7 14.6 1.0 N A:HIS113 4.7 15.1 1.0 C A:HIS113 4.8 15.3 1.0 CD2 A:HIS79 4.8 12.0 1.0 N A:HIS122 4.8 14.3 1.0 N A:ASP125 4.8 15.3 1.0 O A:GLN112 5.0 17.6 1.0

Zinc binding site 2 out of 2 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91E, K94E Double Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91E, K94E Double Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:16.5 occ:1.00 OD1 B:ASP125 1.9 15.3 1.0 ND1 B:HIS104 2.1 19.7 1.0 ND1 B:HIS113 2.1 16.2 1.0 ND1 B:HIS122 2.1 15.7 1.0 CG B:ASP125 2.7 14.7 1.0 OD2 B:ASP125 2.8 13.9 1.0 CE1 B:HIS104 2.9 20.5 1.0 CE1 B:HIS113 3.0 18.1 1.0 CG B:HIS122 3.1 18.1 1.0 CE1 B:HIS122 3.1 17.4 1.0 CG B:HIS104 3.1 19.7 1.0 CG B:HIS113 3.2 15.1 1.0 CB B:HIS122 3.4 16.0 1.0 CB B:HIS104 3.6 18.1 1.0 CB B:HIS113 3.6 15.9 1.0 CA B:HIS113 3.7 16.1 1.0 NE2 B:HIS104 4.1 21.0 1.0 CB B:ASP125 4.1 12.2 1.0 NE2 B:HIS113 4.1 17.1 1.0 NE2 B:HIS122 4.2 18.1 1.0 CD2 B:HIS104 4.2 21.5 1.0 CD2 B:HIS122 4.2 17.4 1.0 CD2 B:HIS113 4.3 16.9 1.0 CD2 B:LEU173 4.6 28.8 1.0 N B:GLY114 4.6 15.1 1.0 CA B:ASP125 4.7 12.0 1.0 CA B:HIS122 4.7 15.9 1.0 C B:HIS113 4.7 15.9 1.0 N B:HIS113 4.7 16.1 1.0 N B:ASP125 4.8 12.9 1.0 N B:HIS122 4.9 14.7 1.0 O B:GLN112 4.9 15.7 1.0 CD2 B:HIS79 4.9 16.9 1.0

M.Didonato, C.J.Kassmann, C.K.Bruns, D.E.Cabelli, Z.Cao, L.B.Tabatabai, J.S.Kroll, E.D.Getzoff. Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91E, K94E Double Mutant To Be Published.