Copper 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:

Zinc

(Zn)

2 atoms

The binding sites of Copper 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 Copper atom.
In total 3 binding sites of Copper where determined in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91E, K94E Double Mutant, PDB code: 2aqs:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91E, K94E Double Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu 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:Cu200 b:18.1 occ:1.00 NE2 A:HIS81 2.0 15.4 1.0 NE2 A:HIS160 2.0 11.9 1.0 ND1 A:HIS79 2.1 11.8 1.0 CD2 A:HIS160 2.9 13.2 1.0 CE1 A:HIS81 2.9 15.5 1.0 CE1 A:HIS79 3.0 13.3 1.0 CD2 A:HIS81 3.0 15.6 1.0 CE1 A:HIS160 3.0 13.9 1.0 CG A:HIS79 3.1 13.4 1.0 NE2 A:HIS104 3.2 16.4 1.0 CB A:HIS79 3.4 12.9 1.0 CD2 A:HIS104 3.5 17.1 1.0 CB A:MET158 3.8 14.0 1.0 O A:HOH615 3.9 23.4 1.0 CG A:MET158 4.0 12.8 1.0 ND1 A:HIS81 4.1 16.3 1.0 O A:HOH429 4.1 20.9 1.0 CE1 A:HIS104 4.1 14.7 1.0 CG A:HIS160 4.1 13.1 1.0 ND1 A:HIS160 4.1 11.8 1.0 NE2 A:HIS79 4.1 12.4 1.0 CG A:HIS81 4.1 15.6 1.0 CD2 A:HIS79 4.2 12.0 1.0 N A:HIS79 4.3 13.3 1.0 CA A:HIS79 4.3 12.5 1.0 CG A:HIS104 4.5 17.3 1.0 O A:HIS79 4.6 14.9 1.0 C A:HIS79 4.7 13.9 1.0 O A:MET158 4.7 14.9 1.0 ND1 A:HIS104 4.8 13.8 1.0 CA A:MET158 4.9 13.7 1.0 C A:MET158 5.0 14.4 1.0

Copper binding site 2 out of 3 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91E, K94E Double Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu 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 A:Cu300 b:36.5 occ:1.00 OE1 A:GLU73 1.9 35.9 1.0 OE1 B:GLU73 2.1 38.1 1.0 ND1 A:HIS133 2.1 33.2 1.0 ND1 B:HIS133 2.2 35.7 1.0 CD A:GLU73 2.6 34.0 1.0 OE2 A:GLU73 2.6 38.9 1.0 CD B:GLU73 2.8 36.4 1.0 OE2 B:GLU73 2.8 39.5 1.0 CE1 A:HIS133 2.8 33.2 1.0 CE1 B:HIS133 2.9 36.8 1.0 CG B:HIS133 3.2 33.9 1.0 CG A:HIS133 3.2 29.9 1.0 CB B:HIS133 3.7 31.1 1.0 CB A:HIS133 3.8 29.6 1.0 NE2 A:HIS133 4.0 33.6 1.0 NE2 B:HIS133 4.0 35.6 1.0 CG A:GLU73 4.1 32.9 1.0 CD2 B:HIS133 4.2 34.7 1.0 CD2 A:HIS133 4.2 32.6 1.0 CA A:HIS133 4.2 28.6 1.0 CG B:GLU73 4.2 34.7 1.0 O B:HOH468 4.3 24.9 1.0 CA B:HIS133 4.3 29.4 1.0 O A:HOH464 4.5 25.6 1.0 CB A:GLU73 4.6 28.9 1.0 CB B:GLU73 4.9 30.3 1.0 N B:HIS133 5.0 27.8 1.0

Copper binding site 3 out of 3 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91E, K94E Double Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91E, K94E Double Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu200 b:21.9 occ:1.00 NE2 B:HIS81 2.0 17.3 1.0 NE2 B:HIS160 2.1 18.7 1.0 ND1 B:HIS79 2.1 17.4 1.0 CE1 B:HIS81 2.9 18.7 1.0 CD2 B:HIS160 3.0 16.7 1.0 CE1 B:HIS79 3.1 17.8 1.0 CD2 B:HIS81 3.1 16.7 1.0 CE1 B:HIS160 3.1 19.6 1.0 CG B:HIS79 3.1 16.9 1.0 NE2 B:HIS104 3.4 21.0 1.0 O B:HOH522 3.5 35.0 1.0 CB B:HIS79 3.5 16.6 1.0 CB B:MET158 3.7 18.4 1.0 CD2 B:HIS104 3.8 21.5 1.0 CG B:MET158 3.9 18.6 1.0 ND1 B:HIS81 4.1 18.2 1.0 CG B:HIS160 4.1 18.3 1.0 ND1 B:HIS160 4.2 17.6 1.0 NE2 B:HIS79 4.2 18.0 1.0 CG B:HIS81 4.2 16.9 1.0 CD2 B:HIS79 4.2 16.9 1.0 CE1 B:HIS104 4.3 20.5 1.0 N B:HIS79 4.4 14.7 1.0 CA B:HIS79 4.4 15.1 1.0 O B:HIS79 4.6 15.2 1.0 O B:MET158 4.7 16.9 1.0 C B:HIS79 4.7 15.6 1.0 O B:HOH485 4.7 31.4 1.0 CG B:HIS104 4.8 19.7 1.0 CA B:MET158 4.9 17.6 1.0 C B:MET158 4.9 17.3 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.