Copper in PDB 2aqp: Cu/Zn Superoxide Dismutase From Neisseria Meningitidis E73A Mutant

All present enzymatic activity of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis E73A Mutant:
1.15.1.1;

The structure of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis E73A Mutant, PDB code: 2aqp 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)	40.00 / 1.30
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	145.874, 48.697, 49.042, 90.00, 109.57, 90.00
R / Rfree (%)	13.5 / 18.3

The structure of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis E73A 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 E73A Mutant (pdb code 2aqp). 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 E73A Mutant, PDB code: 2aqp:
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 E73A 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 E73A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu200 b:15.9 occ:1.00 NE2 A:HIS81 1.9 15.6 1.0 ND1 A:HIS79 1.9 14.7 1.0 NE2 A:HIS160 2.0 14.1 1.0 CE1 A:HIS81 2.9 17.4 1.0 CE1 A:HIS79 2.9 15.3 1.0 CD2 A:HIS81 3.0 16.4 1.0 CD2 A:HIS160 3.0 13.2 1.0 CG A:HIS79 3.0 15.7 1.0 CE1 A:HIS160 3.1 14.1 1.0 NE2 A:HIS104 3.2 20.2 1.0 CB A:HIS79 3.4 16.6 1.0 CD2 A:HIS104 3.6 20.4 1.0 CB A:MET158 3.8 16.1 1.0 O A:HOH461 4.0 19.1 1.0 CE1 A:HIS104 4.0 18.9 1.0 O A:HOH638 4.0 25.2 1.0 CG A:MET158 4.0 16.1 1.0 ND1 A:HIS81 4.0 16.9 1.0 NE2 A:HIS79 4.1 14.7 1.0 CD2 A:HIS79 4.1 15.8 1.0 CG A:HIS81 4.1 15.5 1.0 CG A:HIS160 4.1 13.2 1.0 ND1 A:HIS160 4.2 14.1 1.0 CA A:HIS79 4.3 14.7 1.0 N A:HIS79 4.3 13.2 1.0 CG A:HIS104 4.5 19.4 1.0 O A:HIS79 4.6 15.8 1.0 C A:HIS79 4.7 15.2 1.0 ND1 A:HIS104 4.7 18.6 1.0 O A:MET158 4.8 15.3 1.0

Copper binding site 2 out of 3 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis E73A 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 E73A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu250 b:36.7 occ:0.91 O A:HOH779 2.0 39.4 1.0 ND1 A:HIS148 2.2 28.6 1.0 CE1 A:HIS148 3.1 30.5 1.0 CG A:HIS148 3.3 26.8 1.0 OE2 A:GLU57 3.4 26.8 1.0 CB A:HIS148 3.5 25.1 1.0 O A:HOH755 3.8 42.5 1.0 CD A:GLU57 4.0 24.0 1.0 CA A:HIS148 4.0 23.6 1.0 OE1 A:GLU57 4.1 23.7 1.0 NE2 A:HIS148 4.3 28.9 1.0 O A:HOH714 4.3 36.8 1.0 O A:LYS147 4.3 26.0 1.0 CD2 A:HIS148 4.4 25.9 1.0 O A:HOH713 4.4 35.8 1.0 O A:HOH625 4.9 28.5 1.0 N A:HIS148 5.0 21.8 1.0

Copper binding site 3 out of 3 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis E73A 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 E73A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu200 b:16.0 occ:1.00 NE2 B:HIS81 1.9 15.7 1.0 ND1 B:HIS79 2.0 14.2 1.0 NE2 B:HIS160 2.1 15.3 1.0 CE1 B:HIS81 2.9 16.1 1.0 CD2 B:HIS81 2.9 15.7 1.0 CD2 B:HIS160 3.0 13.9 1.0 CG B:HIS79 3.0 15.2 1.0 CE1 B:HIS79 3.0 13.9 1.0 CE1 B:HIS160 3.1 14.6 1.0 NE2 B:HIS104 3.2 18.5 1.0 CB B:HIS79 3.3 15.8 1.0 CD2 B:HIS104 3.6 18.7 1.0 CB B:MET158 3.8 15.6 1.0 CE1 B:HIS104 4.0 18.1 1.0 O B:HOH449 4.0 20.1 1.0 ND1 B:HIS81 4.1 17.4 1.0 CG B:MET158 4.1 15.8 1.0 O B:HOH672 4.1 27.4 1.0 NE2 B:HIS79 4.1 13.9 1.0 CG B:HIS81 4.1 15.3 1.0 CD2 B:HIS79 4.1 16.1 1.0 CG B:HIS160 4.1 13.4 1.0 ND1 B:HIS160 4.2 13.8 1.0 CA B:HIS79 4.3 15.0 1.0 N B:HIS79 4.4 13.5 1.0 CG B:HIS104 4.5 18.4 1.0 O B:HIS79 4.6 15.9 1.0 ND1 B:HIS104 4.7 19.8 1.0 C B:HIS79 4.8 15.2 1.0 O B:MET158 4.8 14.9 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 E73A Mutant To Be Published.