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Manganese in PDB 1ar4: X-Ray Structure Analysis of the Cambialistic Superoxide Dismutase From Propionibacterium Shermanii Active with Fe or Mn

Enzymatic activity of X-Ray Structure Analysis of the Cambialistic Superoxide Dismutase From Propionibacterium Shermanii Active with Fe or Mn

All present enzymatic activity of X-Ray Structure Analysis of the Cambialistic Superoxide Dismutase From Propionibacterium Shermanii Active with Fe or Mn:
1.15.1.1;

Protein crystallography data

The structure of X-Ray Structure Analysis of the Cambialistic Superoxide Dismutase From Propionibacterium Shermanii Active with Fe or Mn, PDB code: 1ar4 was solved by M.Schmidt, B.Meier, F.Parak, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 9.00 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 79.680, 85.640, 108.850, 90.00, 90.00, 90.00
R / Rfree (%) 15.6 / 20.5

Manganese Binding Sites:

The binding sites of Manganese atom in the X-Ray Structure Analysis of the Cambialistic Superoxide Dismutase From Propionibacterium Shermanii Active with Fe or Mn (pdb code 1ar4). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the X-Ray Structure Analysis of the Cambialistic Superoxide Dismutase From Propionibacterium Shermanii Active with Fe or Mn, PDB code: 1ar4:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1ar4

Go back to Manganese Binding Sites List in 1ar4
Manganese binding site 1 out of 2 in the X-Ray Structure Analysis of the Cambialistic Superoxide Dismutase From Propionibacterium Shermanii Active with Fe or Mn


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of X-Ray Structure Analysis of the Cambialistic Superoxide Dismutase From Propionibacterium Shermanii Active with Fe or Mn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn202

b:8.8
occ:1.00
OD2 A:ASP161 1.9 7.8 1.0
NE2 A:HIS27 2.1 6.9 1.0
NE2 A:HIS75 2.2 8.0 1.0
NE2 A:HIS165 2.2 6.0 1.0
O A:HOH203 2.3 9.0 1.0
CG A:ASP161 3.0 9.6 1.0
CD2 A:HIS27 3.1 6.7 1.0
CE1 A:HIS75 3.1 3.4 1.0
CE1 A:HIS27 3.2 6.0 1.0
CD2 A:HIS165 3.2 10.5 1.0
CD2 A:HIS75 3.2 4.2 1.0
CE1 A:HIS165 3.2 7.5 1.0
OD1 A:ASP161 3.6 6.9 1.0
CG A:HIS27 4.2 6.5 1.0
ND1 A:HIS75 4.2 5.8 1.0
ND1 A:HIS27 4.2 6.7 1.0
CB A:ASP161 4.3 6.8 1.0
CG A:HIS75 4.3 5.3 1.0
ND1 A:HIS165 4.3 9.5 1.0
CG A:HIS165 4.3 11.6 1.0
CZ2 A:TRP126 4.4 5.0 1.0
CB A:TRP163 4.6 5.2 1.0
CH2 A:TRP126 4.7 4.1 1.0
CB A:ALA166 4.8 4.8 1.0
CG A:TRP163 4.8 9.7 1.0

Manganese binding site 2 out of 2 in 1ar4

Go back to Manganese Binding Sites List in 1ar4
Manganese binding site 2 out of 2 in the X-Ray Structure Analysis of the Cambialistic Superoxide Dismutase From Propionibacterium Shermanii Active with Fe or Mn


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of X-Ray Structure Analysis of the Cambialistic Superoxide Dismutase From Propionibacterium Shermanii Active with Fe or Mn within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn202

b:9.0
occ:1.00
OD2 B:ASP161 1.9 8.9 1.0
NE2 B:HIS75 2.1 7.4 1.0
NE2 B:HIS165 2.1 5.5 1.0
NE2 B:HIS27 2.2 8.5 1.0
O B:HOH203 2.3 8.5 1.0
CE1 B:HIS75 3.0 7.5 1.0
CG B:ASP161 3.0 11.7 1.0
CE1 B:HIS165 3.1 5.5 1.0
CD2 B:HIS27 3.1 5.1 1.0
CD2 B:HIS165 3.1 4.4 1.0
CE1 B:HIS27 3.2 9.0 1.0
CD2 B:HIS75 3.2 5.7 1.0
OD1 B:ASP161 3.5 10.2 1.0
ND1 B:HIS75 4.2 8.5 1.0
ND1 B:HIS165 4.2 6.3 1.0
ND1 B:HIS27 4.3 8.5 1.0
CG B:HIS75 4.3 6.7 1.0
CG B:HIS165 4.3 5.8 1.0
CG B:HIS27 4.3 9.3 1.0
CB B:ASP161 4.3 7.6 1.0
CZ2 B:TRP126 4.5 13.3 1.0
CB B:TRP163 4.6 5.9 1.0
CB B:ALA166 4.8 8.7 1.0
CG B:TRP163 4.8 7.3 1.0
CH2 B:TRP126 4.8 5.8 1.0
NE2 B:HIS146 5.0 8.4 1.0

Reference:

M.Schmidt, B.Meier, F.Parak. X-Ray Structure of the Cambialistic Superoxide Dismutase From Propionibacterium Shermanii Active with Fe or Mn J.Biol.Inorg.Chem. V. 1 532 1996.
ISSN: ISSN 0949-8257
Page generated: Sat Oct 5 09:44:47 2024

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