Zinc 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:

Copper

(Cu)

3 atoms

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc where determined in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis E73A Mutant, PDB code: 2aqp:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis E73A 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 E73A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:16.7 occ:1.00 OD1 A:ASP125 1.9 17.2 1.0 ND1 A:HIS104 2.0 18.6 1.0 ND1 A:HIS122 2.0 17.0 1.0 ND1 A:HIS113 2.0 16.8 1.0 CG A:ASP125 2.7 17.1 1.0 OD2 A:ASP125 2.9 17.4 1.0 CE1 A:HIS113 2.9 15.7 1.0 CE1 A:HIS104 2.9 18.9 1.0 CE1 A:HIS122 3.0 18.8 1.0 CG A:HIS104 3.1 19.4 1.0 CG A:HIS122 3.1 17.4 1.0 CG A:HIS113 3.1 15.4 1.0 CB A:HIS104 3.5 21.1 1.0 CB A:HIS122 3.5 20.3 1.0 CB A:HIS113 3.6 17.1 1.0 CA A:HIS113 3.8 17.6 1.0 NE2 A:HIS104 4.1 20.2 1.0 NE2 A:HIS113 4.1 15.5 1.0 CB A:ASP125 4.1 15.7 1.0 NE2 A:HIS122 4.1 20.4 1.0 CD2 A:HIS104 4.2 20.4 1.0 CD2 A:HIS122 4.2 21.6 1.0 CD2 A:HIS113 4.2 15.7 1.0 CD2 A:LEU173 4.5 22.2 1.0 CA A:ASP125 4.6 16.0 1.0 N A:GLY114 4.7 17.1 1.0 N A:HIS113 4.7 19.1 1.0 C A:HIS113 4.8 18.8 1.0 CA A:HIS122 4.8 20.8 1.0 N A:ASP125 4.8 16.3 1.0 CD2 A:HIS79 4.8 15.8 1.0 O A:GLN112 4.9 21.6 1.0 CA A:HIS104 5.0 20.2 1.0 N A:HIS122 5.0 19.8 1.0

Zinc binding site 2 out of 2 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis E73A 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 E73A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:17.1 occ:1.00 OD1 B:ASP125 2.0 17.0 1.0 ND1 B:HIS122 2.0 16.9 1.0 ND1 B:HIS104 2.0 19.8 1.0 ND1 B:HIS113 2.0 16.0 1.0 CG B:ASP125 2.7 17.3 1.0 OD2 B:ASP125 2.9 16.8 1.0 CE1 B:HIS113 2.9 16.1 1.0 CE1 B:HIS104 3.0 18.1 1.0 CE1 B:HIS122 3.0 19.5 1.0 CG B:HIS104 3.1 18.4 1.0 CG B:HIS122 3.1 18.8 1.0 CG B:HIS113 3.2 15.9 1.0 CB B:HIS104 3.5 20.7 1.0 CB B:HIS122 3.5 20.3 1.0 CB B:HIS113 3.6 17.7 1.0 CA B:HIS113 3.8 17.0 1.0 NE2 B:HIS104 4.1 18.5 1.0 NE2 B:HIS122 4.1 21.6 1.0 NE2 B:HIS113 4.1 15.5 1.0 CB B:ASP125 4.1 15.6 1.0 CD2 B:HIS104 4.2 18.7 1.0 CD2 B:HIS122 4.2 21.9 1.0 CD2 B:HIS113 4.2 15.3 1.0 CD2 B:LEU173 4.5 22.7 1.0 N B:GLY114 4.7 16.9 1.0 CA B:ASP125 4.7 16.6 1.0 N B:HIS113 4.7 19.9 1.0 C B:HIS113 4.8 17.3 1.0 CA B:HIS122 4.8 20.4 1.0 CD2 B:HIS79 4.9 16.1 1.0 N B:ASP125 4.9 17.0 1.0 O B:GLN112 4.9 22.1 1.0 N B:HIS122 4.9 20.7 1.0 CA B:HIS104 5.0 20.2 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.