Manganese in PDB 3evk: Crystal Structure of the Metal-Bound Superoxide Dismutase From Pyrobaculum Aerophilum

All present enzymatic activity of Crystal Structure of the Metal-Bound Superoxide Dismutase From Pyrobaculum Aerophilum:
1.15.1.1;

The structure of Crystal Structure of the Metal-Bound Superoxide Dismutase From Pyrobaculum Aerophilum, PDB code: 3evk was solved by S.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.54 / 1.85
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	94.909, 94.909, 171.890, 90.00, 90.00, 120.00
R / Rfree (%)	20.2 / 23

The binding sites of Manganese atom in the Crystal Structure of the Metal-Bound Superoxide Dismutase From Pyrobaculum Aerophilum (pdb code 3evk). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure of the Metal-Bound Superoxide Dismutase From Pyrobaculum Aerophilum, PDB code: 3evk:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Crystal Structure of the Metal-Bound Superoxide Dismutase From Pyrobaculum Aerophilum


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of the Metal-Bound Superoxide Dismutase From Pyrobaculum Aerophilum within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn301 b:33.2 occ:1.00 O A:HOH302 2.0 21.5 1.0 OD2 A:ASP176 2.0 30.5 1.0 NE2 A:HIS42 2.3 31.9 1.0 NE2 A:HIS90 2.3 29.7 1.0 NE2 A:HIS180 2.4 30.4 1.0 CE1 A:HIS90 3.1 29.8 1.0 CG A:ASP176 3.1 28.4 1.0 CD2 A:HIS42 3.1 30.9 1.0 CD2 A:HIS180 3.2 30.3 1.0 CE1 A:HIS42 3.3 31.6 1.0 CD2 A:HIS90 3.4 30.0 1.0 CE1 A:HIS180 3.5 31.3 1.0 OD1 A:ASP176 3.5 29.3 1.0 ND1 A:HIS90 4.3 27.5 1.0 CG A:HIS42 4.3 30.4 1.0 ND1 A:HIS42 4.3 30.8 1.0 CB A:TRP178 4.3 28.4 1.0 CB A:ASP176 4.4 28.2 1.0 CG A:HIS180 4.4 29.8 1.0 CG A:HIS90 4.5 29.4 1.0 ND1 A:HIS180 4.5 30.2 1.0 CG A:TRP178 4.5 28.2 1.0 CZ2 A:TRP141 4.6 27.5 1.0 CD1 A:TRP178 4.8 28.4 1.0 NE2 A:HIS161 4.8 30.0 1.0 CE2 A:TYR50 4.8 31.0 1.0 CH2 A:TRP141 4.8 28.4 1.0 OH A:TYR50 4.9 33.4 1.0 CB A:ALA181 4.9 28.2 1.0

Manganese binding site 2 out of 4 in the Crystal Structure of the Metal-Bound Superoxide Dismutase From Pyrobaculum Aerophilum


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of the Metal-Bound Superoxide Dismutase From Pyrobaculum Aerophilum within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn301 b:48.9 occ:1.00 OD2 B:ASP176 1.7 31.7 1.0 NE2 B:HIS42 2.1 29.7 1.0 O B:HOH302 2.2 36.9 1.0 NE2 B:HIS90 2.5 33.0 1.0 NE2 B:HIS180 2.5 31.9 1.0 CG B:ASP176 2.9 30.3 1.0 CE1 B:HIS42 3.1 29.4 1.0 CD2 B:HIS42 3.1 29.9 1.0 CE1 B:HIS90 3.3 32.6 1.0 CD2 B:HIS180 3.3 32.1 1.0 OD1 B:ASP176 3.4 32.4 1.0 CE1 B:HIS180 3.5 32.5 1.0 CD2 B:HIS90 3.6 31.8 1.0 CB B:ASP176 4.1 29.8 1.0 ND1 B:HIS42 4.2 30.7 1.0 CG B:HIS42 4.2 30.1 1.0 CB B:TRP178 4.3 29.4 1.0 ND1 B:HIS90 4.4 32.4 1.0 CG B:HIS180 4.5 30.7 1.0 CG B:TRP178 4.5 29.6 1.0 ND1 B:HIS180 4.5 31.9 1.0 CB B:ALA181 4.6 28.9 1.0 CZ2 B:TRP141 4.6 28.1 1.0 CG B:HIS90 4.6 31.6 1.0 CD1 B:TRP178 4.8 29.4 1.0 CH2 B:TRP141 4.9 27.4 1.0

Manganese binding site 3 out of 4 in the Crystal Structure of the Metal-Bound Superoxide Dismutase From Pyrobaculum Aerophilum


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of the Metal-Bound Superoxide Dismutase From Pyrobaculum Aerophilum within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn301 b:35.0 occ:1.00 O C:HOH302 1.9 15.0 1.0 OD2 C:ASP176 2.1 30.9 1.0 NE2 C:HIS42 2.1 31.1 1.0 NE2 C:HIS90 2.4 29.5 1.0 NE2 C:HIS180 2.4 29.4 1.0 CE1 C:HIS90 3.0 28.8 1.0 CD2 C:HIS42 3.0 29.6 1.0 CE1 C:HIS42 3.1 29.9 1.0 CG C:ASP176 3.1 29.5 1.0 CD2 C:HIS180 3.2 29.1 1.0 CE1 C:HIS180 3.5 30.5 1.0 OD1 C:ASP176 3.5 28.4 1.0 CD2 C:HIS90 3.6 30.0 1.0 CG C:HIS42 4.2 28.1 1.0 ND1 C:HIS42 4.2 28.3 1.0 ND1 C:HIS90 4.3 29.2 1.0 CB C:TRP178 4.3 28.0 1.0 CG C:HIS180 4.4 28.4 1.0 CB C:ASP176 4.4 29.0 1.0 ND1 C:HIS180 4.5 31.2 1.0 CG C:HIS90 4.6 29.5 1.0 CG C:TRP178 4.6 28.7 1.0 CZ2 C:TRP141 4.6 30.0 1.0 CB C:ALA181 4.8 29.1 1.0 OH C:TYR50 4.8 32.2 1.0 CE2 C:TYR50 4.8 29.4 1.0 CD1 C:TRP178 4.9 29.0 1.0 NE2 C:HIS161 4.9 30.1 1.0 CH2 C:TRP141 4.9 28.9 1.0 CB C:HIS46 5.0 29.6 1.0

Manganese binding site 4 out of 4 in the Crystal Structure of the Metal-Bound Superoxide Dismutase From Pyrobaculum Aerophilum


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of the Metal-Bound Superoxide Dismutase From Pyrobaculum Aerophilum within 5.0Å range: probe atom residue distance (Å) B Occ D:Mn301 b:47.1 occ:1.00 NE2 D:HIS90 2.1 30.6 1.0 NE2 D:HIS42 2.3 27.6 1.0 NE2 D:HIS180 2.3 30.9 1.0 OD2 D:ASP176 2.5 25.5 1.0 CE1 D:HIS90 2.8 29.5 1.0 CD2 D:HIS42 3.0 28.2 1.0 CD2 D:HIS90 3.3 29.9 1.0 CD2 D:HIS180 3.3 31.2 1.0 CE1 D:HIS180 3.3 32.1 1.0 CE1 D:HIS42 3.5 28.9 1.0 CG D:ASP176 3.6 27.5 1.0 ND1 D:HIS90 4.1 30.5 1.0 OD1 D:ASP176 4.1 26.1 1.0 CG D:HIS42 4.2 28.8 1.0 CG D:HIS90 4.3 30.3 1.0 CE2 D:TYR50 4.4 31.3 1.0 ND1 D:HIS180 4.4 31.4 1.0 ND1 D:HIS42 4.4 28.1 1.0 CG D:HIS180 4.5 30.0 1.0 OH D:TYR50 4.5 32.2 1.0 CB D:HIS46 4.7 30.1 1.0 CZ2 D:TRP141 4.7 28.1 1.0 NE2 D:HIS161 4.7 30.6 1.0 CB D:ASP176 4.8 27.4 1.0 CB D:TRP178 4.8 28.9 1.0 CG D:TRP178 4.9 28.6 1.0 CZ D:TYR50 5.0 31.8 1.0

S.Lee, S.Lee. N/A N/A.
ISSN: ISSN 0253-2964