Zinc in PDB 2aqt: Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant

All present enzymatic activity of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant:
1.15.1.1;

The structure of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant, PDB code: 2aqt 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)	49.44 / 1.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	98.209, 64.464, 85.051, 90.00, 128.33, 90.00
R / Rfree (%)	18.5 / 21.5

The structure of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant also contains other interesting chemical elements:

Copper

(Cu)

5 atoms

The binding sites of Zinc atom in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant (pdb code 2aqt). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant, PDB code: 2aqt:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q 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 K91Q, K94Q Double Mutant within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn201 b:15.8 occ:1.00 OD1 C:ASP125 2.0 11.8 1.0 ND1 C:HIS104 2.0 15.6 1.0 ND1 C:HIS122 2.1 15.2 1.0 ND1 C:HIS113 2.1 13.8 1.0 CG C:ASP125 2.7 12.3 1.0 OD2 C:ASP125 2.9 12.1 1.0 CE1 C:HIS104 2.9 14.5 1.0 CE1 C:HIS113 3.0 14.8 1.0 CE1 C:HIS122 3.1 17.2 1.0 CG C:HIS122 3.1 16.7 1.0 CG C:HIS104 3.1 14.9 1.0 CG C:HIS113 3.2 15.3 1.0 CB C:HIS122 3.4 16.3 1.0 CB C:HIS104 3.5 15.9 1.0 CB C:HIS113 3.6 15.5 1.0 CA C:HIS113 3.8 16.3 1.0 NE2 C:HIS104 4.1 16.0 1.0 CB C:ASP125 4.2 12.5 1.0 CD2 C:HIS104 4.2 15.3 1.0 NE2 C:HIS122 4.2 17.1 1.0 NE2 C:HIS113 4.2 13.9 1.0 CD2 C:HIS122 4.2 15.9 1.0 CD2 C:HIS113 4.3 13.6 1.0 CD2 C:LEU173 4.7 21.5 1.0 CA C:ASP125 4.7 13.1 1.0 CA C:HIS122 4.7 14.5 1.0 N C:GLY114 4.7 16.9 1.0 N C:HIS113 4.7 17.5 1.0 C C:HIS113 4.8 17.4 1.0 N C:HIS122 4.8 15.5 1.0 N C:ASP125 4.8 12.8 1.0 O C:GLN112 4.8 18.8 1.0 CD2 C:HIS79 4.8 13.2 1.0 CA C:HIS104 5.0 16.1 1.0

Zinc binding site 2 out of 3 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q 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 K91Q, K94Q Double Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:23.8 occ:1.00 OD1 B:ASP125 1.9 18.9 1.0 ND1 B:HIS104 2.0 22.2 1.0 ND1 B:HIS113 2.0 25.1 1.0 ND1 B:HIS122 2.1 25.4 1.0 CG B:ASP125 2.7 21.0 1.0 OD2 B:ASP125 2.7 21.6 1.0 CE1 B:HIS113 2.9 24.0 1.0 CE1 B:HIS104 2.9 25.0 1.0 CG B:HIS104 3.1 25.7 1.0 CG B:HIS122 3.1 26.4 1.0 CE1 B:HIS122 3.1 26.9 1.0 CG B:HIS113 3.1 24.5 1.0 CB B:HIS122 3.4 24.1 1.0 CB B:HIS104 3.5 23.2 1.0 CB B:HIS113 3.6 25.3 1.0 CA B:HIS113 3.8 25.8 1.0 NE2 B:HIS104 4.0 25.4 1.0 NE2 B:HIS113 4.0 24.6 1.0 CB B:ASP125 4.1 20.8 1.0 CD2 B:HIS104 4.1 24.8 1.0 CD2 B:HIS113 4.2 24.6 1.0 NE2 B:HIS122 4.2 26.5 1.0 CD2 B:HIS122 4.2 26.8 1.0 CA B:ASP125 4.6 21.4 1.0 N B:HIS113 4.7 27.7 1.0 CA B:HIS122 4.7 25.1 1.0 N B:GLY114 4.7 23.8 1.0 C B:HIS113 4.8 25.1 1.0 N B:HIS122 4.8 24.6 1.0 CD2 B:LEU173 4.8 26.3 1.0 N B:ASP125 4.8 20.5 1.0 CD2 B:HIS79 4.9 19.0 1.0 O B:GLN112 4.9 29.0 1.0 CA B:HIS104 5.0 24.4 1.0

Zinc binding site 3 out of 3 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:18.9 occ:1.00 OD1 A:ASP125 1.9 17.1 1.0 ND1 A:HIS104 2.1 18.0 1.0 ND1 A:HIS113 2.1 18.2 1.0 ND1 A:HIS122 2.2 18.5 1.0 CG A:ASP125 2.7 17.7 1.0 OD2 A:ASP125 2.9 17.6 1.0 CE1 A:HIS113 2.9 18.2 1.0 CE1 A:HIS104 3.0 21.7 1.0 CG A:HIS122 3.1 20.5 1.0 CG A:HIS104 3.1 20.5 1.0 CE1 A:HIS122 3.2 20.5 1.0 CG A:HIS113 3.2 19.7 1.0 CB A:HIS122 3.3 18.8 1.0 CB A:HIS104 3.5 20.0 1.0 CB A:HIS113 3.6 19.5 1.0 CA A:HIS113 3.8 18.5 1.0 NE2 A:HIS113 4.1 18.0 1.0 NE2 A:HIS104 4.1 21.5 1.0 CB A:ASP125 4.1 18.0 1.0 CD2 A:HIS104 4.2 20.4 1.0 CD2 A:HIS113 4.2 20.1 1.0 CD2 A:HIS122 4.3 16.7 1.0 NE2 A:HIS122 4.3 18.3 1.0 CD2 A:LEU173 4.5 24.7 1.0 CA A:HIS122 4.7 19.3 1.0 N A:GLY114 4.7 19.1 1.0 CA A:ASP125 4.7 15.3 1.0 N A:HIS113 4.7 18.9 1.0 C A:HIS113 4.8 18.6 1.0 CD2 A:HIS79 4.8 17.7 1.0 N A:HIS122 4.8 19.4 1.0 N A:ASP125 4.8 15.1 1.0 O A:GLN112 4.9 17.8 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 K91Q, K94Q Double Mutant To Be Published.