Manganese in PDB 2qka: Structural and Kinetic Study of the Differences Between Human and E.Coli Manganese Superoxide Dismutases

All present enzymatic activity of Structural and Kinetic Study of the Differences Between Human and E.Coli Manganese Superoxide Dismutases:
1.15.1.1;

The structure of Structural and Kinetic Study of the Differences Between Human and E.Coli Manganese Superoxide Dismutases, PDB code: 2qka was solved by J.Zheng, J.F.Domsic, D.Cabelli, R.Mckenna, D.N.Silverman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.20
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	81.162, 81.162, 242.771, 90.00, 90.00, 120.00
R / Rfree (%)	19.5 / 21.7

The binding sites of Manganese atom in the Structural and Kinetic Study of the Differences Between Human and E.Coli Manganese Superoxide Dismutases (pdb code 2qka). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Structural and Kinetic Study of the Differences Between Human and E.Coli Manganese Superoxide Dismutases, PDB code: 2qka:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Structural and Kinetic Study of the Differences Between Human and E.Coli Manganese Superoxide Dismutases


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structural and Kinetic Study of the Differences Between Human and E.Coli Manganese Superoxide Dismutases within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn199 b:17.1 occ:1.00 OD2 A:ASP159 1.9 15.4 1.0 O A:HOH240 2.2 14.7 1.0 NE2 A:HIS26 2.2 14.1 1.0 NE2 A:HIS74 2.2 14.0 1.0 NE2 A:HIS163 2.3 14.8 1.0 CG A:ASP159 3.0 16.4 1.0 CE1 A:HIS26 3.1 14.5 1.0 CE1 A:HIS74 3.2 12.5 1.0 CD2 A:HIS26 3.2 14.0 1.0 CD2 A:HIS74 3.2 13.2 1.0 CD2 A:HIS163 3.2 13.5 1.0 CE1 A:HIS163 3.3 13.3 1.0 OD1 A:ASP159 3.5 17.2 1.0 ND1 A:HIS26 4.3 16.4 1.0 ND1 A:HIS74 4.3 13.4 1.0 CB A:ASP159 4.3 15.5 1.0 CZ2 A:TRP123 4.3 13.8 1.0 CG A:HIS26 4.3 16.6 1.0 CG A:HIS74 4.3 13.7 1.0 ND1 A:HIS163 4.4 13.9 1.0 CG A:HIS163 4.4 15.8 1.0 NE2 A:GLN143 4.6 12.9 1.0 CB A:TRP161 4.6 13.6 1.0 CG A:TRP161 4.8 13.4 1.0 CH2 A:TRP123 4.8 14.6 1.0 CB A:ALA164 4.9 15.6 1.0

Manganese binding site 2 out of 2 in the Structural and Kinetic Study of the Differences Between Human and E.Coli Manganese Superoxide Dismutases


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structural and Kinetic Study of the Differences Between Human and E.Coli Manganese Superoxide Dismutases within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn199 b:16.3 occ:1.00 OD2 C:ASP159 1.9 13.2 1.0 O C:HOH314 2.2 16.9 1.0 NE2 C:HIS26 2.2 17.2 1.0 NE2 C:HIS74 2.2 15.7 1.0 NE2 C:HIS163 2.3 18.2 1.0 CG C:ASP159 3.0 14.8 1.0 CE1 C:HIS26 3.1 16.8 1.0 CE1 C:HIS74 3.2 12.2 1.0 CD2 C:HIS26 3.2 15.7 1.0 CD2 C:HIS74 3.2 13.7 1.0 CD2 C:HIS163 3.2 15.4 1.0 CE1 C:HIS163 3.3 16.8 1.0 OD1 C:ASP159 3.5 14.9 1.0 ND1 C:HIS26 4.3 16.2 1.0 ND1 C:HIS74 4.3 12.4 1.0 CB C:ASP159 4.3 15.6 1.0 CZ2 C:TRP123 4.3 12.8 1.0 CG C:HIS26 4.3 16.2 1.0 CG C:HIS74 4.3 15.2 1.0 ND1 C:HIS163 4.4 16.2 1.0 CG C:HIS163 4.4 15.7 1.0 NE2 C:GLN143 4.6 14.4 1.0 CB C:TRP161 4.6 14.2 1.0 CG C:TRP161 4.8 12.2 1.0 CH2 C:TRP123 4.8 12.0 1.0 CB C:ALA164 4.9 13.5 1.0

J.Zheng, J.F.Domsic, D.Cabelli, R.Mckenna, D.N.Silverman. Structural and Kinetic Study of Differences Between Human and Escherichia Coli Manganese Superoxide Dismutases. Biochemistry V. 46 14830 2007.
ISSN: ISSN 0006-2960
PubMed: 18044968
DOI: 10.1021/BI7014103