Zinc in PDB 2aqr: Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant

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

The structure of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant, PDB code: 2aqr 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)	29.47 / 1.75
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	98.840, 65.052, 77.443, 90.00, 121.02, 90.00
R / Rfree (%)	16.9 / 19.7

The structure of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q 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 Mutant (pdb code 2aqr). 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 Mutant, PDB code: 2aqr:
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 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 Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:12.4 occ:1.00 OD1 A:ASP125 1.9 11.0 1.0 ND1 A:HIS104 2.0 10.4 1.0 ND1 A:HIS113 2.1 9.5 1.0 ND1 A:HIS122 2.1 11.1 1.0 CG A:ASP125 2.8 8.9 1.0 CE1 A:HIS113 2.9 10.6 1.0 CE1 A:HIS104 2.9 11.5 1.0 OD2 A:ASP125 3.0 11.4 1.0 CE1 A:HIS122 3.1 12.5 1.0 CG A:HIS122 3.1 12.4 1.0 CG A:HIS104 3.1 11.9 1.0 CG A:HIS113 3.2 12.2 1.0 CB A:HIS122 3.4 11.7 1.0 CB A:HIS104 3.5 10.5 1.0 CB A:HIS113 3.6 12.1 1.0 CA A:HIS113 3.8 11.1 1.0 NE2 A:HIS104 4.1 12.2 1.0 NE2 A:HIS113 4.1 11.5 1.0 NE2 A:HIS122 4.2 12.0 1.0 CD2 A:HIS104 4.2 11.1 1.0 CB A:ASP125 4.2 10.5 1.0 CD2 A:HIS122 4.2 13.1 1.0 CD2 A:HIS113 4.2 10.2 1.0 CD2 A:LEU173 4.6 16.6 1.0 N A:GLY114 4.7 11.9 1.0 CA A:ASP125 4.7 10.2 1.0 CA A:HIS122 4.7 11.8 1.0 C A:HIS113 4.8 13.3 1.0 N A:HIS113 4.8 13.4 1.0 CD2 A:HIS79 4.8 11.0 1.0 N A:ASP125 4.8 10.6 1.0 N A:HIS122 4.8 13.0 1.0 O A:GLN112 4.9 12.8 1.0

Zinc binding site 2 out of 3 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q 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 Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:12.8 occ:1.00 OD1 B:ASP125 1.9 9.6 1.0 ND1 B:HIS104 2.1 11.8 1.0 ND1 B:HIS113 2.1 11.3 1.0 ND1 B:HIS122 2.1 12.4 1.0 CG B:ASP125 2.7 9.7 1.0 OD2 B:ASP125 2.8 9.5 1.0 CE1 B:HIS113 2.9 11.5 1.0 CE1 B:HIS104 3.0 14.8 1.0 CG B:HIS122 3.1 13.8 1.0 CE1 B:HIS122 3.1 15.2 1.0 CG B:HIS104 3.1 14.9 1.0 CG B:HIS113 3.2 11.2 1.0 CB B:HIS122 3.4 11.8 1.0 CB B:HIS104 3.5 13.1 1.0 CB B:HIS113 3.6 12.2 1.0 CA B:HIS113 3.7 12.2 1.0 NE2 B:HIS113 4.1 11.2 1.0 CB B:ASP125 4.1 9.8 1.0 NE2 B:HIS104 4.1 14.5 1.0 CD2 B:HIS104 4.2 13.8 1.0 NE2 B:HIS122 4.2 14.9 1.0 CD2 B:HIS122 4.2 13.1 1.0 CD2 B:HIS113 4.2 12.1 1.0 CD2 B:LEU173 4.6 16.9 1.0 N B:GLY114 4.6 10.8 1.0 CA B:ASP125 4.7 10.2 1.0 CA B:HIS122 4.7 12.7 1.0 N B:HIS113 4.7 12.8 1.0 C B:HIS113 4.7 12.9 1.0 N B:HIS122 4.8 13.1 1.0 N B:ASP125 4.8 10.3 1.0 CD2 B:HIS79 4.9 10.9 1.0 O B:GLN112 4.9 13.3 1.0

Zinc binding site 3 out of 3 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q 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 Mutant within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn201 b:11.9 occ:1.00 OD1 C:ASP125 2.0 8.3 1.0 ND1 C:HIS104 2.0 11.8 1.0 ND1 C:HIS113 2.1 9.1 1.0 ND1 C:HIS122 2.1 9.5 1.0 CG C:ASP125 2.7 9.6 1.0 OD2 C:ASP125 2.8 10.2 1.0 CE1 C:HIS104 2.9 12.1 1.0 CE1 C:HIS113 2.9 11.9 1.0 CE1 C:HIS122 3.1 11.5 1.0 CG C:HIS122 3.1 10.8 1.0 CG C:HIS104 3.1 13.2 1.0 CG C:HIS113 3.2 10.2 1.0 CB C:HIS122 3.4 12.1 1.0 CB C:HIS104 3.5 12.1 1.0 CB C:HIS113 3.6 10.3 1.0 CA C:HIS113 3.8 11.0 1.0 NE2 C:HIS104 4.1 12.5 1.0 NE2 C:HIS113 4.1 10.1 1.0 CB C:ASP125 4.1 9.7 1.0 CD2 C:HIS104 4.2 13.2 1.0 NE2 C:HIS122 4.2 11.2 1.0 CD2 C:HIS122 4.2 11.9 1.0 CD2 C:HIS113 4.3 10.5 1.0 CD2 C:LEU173 4.5 17.4 1.0 N C:GLY114 4.6 10.9 1.0 CA C:ASP125 4.7 9.9 1.0 CA C:HIS122 4.7 10.9 1.0 C C:HIS113 4.8 11.8 1.0 N C:HIS113 4.8 12.1 1.0 CD2 C:HIS79 4.8 8.4 1.0 N C:HIS122 4.8 12.7 1.0 N C:ASP125 4.8 9.6 1.0 O C:GLN112 4.8 11.4 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 Mutant To Be Published.