Manganese in PDB 8a8k: Pap Phosphatase From Methanothermococcus Thermolithotrophicus Refined to 3.1 A

All present enzymatic activity of Pap Phosphatase From Methanothermococcus Thermolithotrophicus Refined to 3.1 A:
3.1.3.7;

The structure of Pap Phosphatase From Methanothermococcus Thermolithotrophicus Refined to 3.1 A, PDB code: 8a8k was solved by M.Jespersen, T.Wagner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	57.79 / 3.10
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	174.054, 174.054, 183.803, 90, 90, 90
R / Rfree (%)	18.6 / 22

The binding sites of Manganese atom in the Pap Phosphatase From Methanothermococcus Thermolithotrophicus Refined to 3.1 A (pdb code 8a8k). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the Pap Phosphatase From Methanothermococcus Thermolithotrophicus Refined to 3.1 A, PDB code: 8a8k:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in the Pap Phosphatase From Methanothermococcus Thermolithotrophicus Refined to 3.1 A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Pap Phosphatase From Methanothermococcus Thermolithotrophicus Refined to 3.1 A within 5.0Å range: probe atom residue distance (Å) B Occ D:Mn402 b:86.6 occ:0.54 OD2 D:ASP57 2.6 80.5 1.0 OD1 D:ASP57 2.6 90.3 1.0 OD2 D:ASP127 2.8 86.6 1.0 OD2 D:ASP10 2.9 77.2 1.0 OD1 D:ASP127 2.9 108.0 1.0 CG D:ASP57 3.0 84.3 1.0 CG D:ASP127 3.2 92.1 1.0 CE1 D:HIS76 3.4 84.0 1.0 O3' D:AMP401 3.4 110.1 1.0 CG D:ASP10 3.7 71.0 1.0 CB D:ASP10 3.8 70.2 1.0 OD2 D:ASP8 3.8 81.5 1.0 CE1 D:HIS77 4.0 99.3 1.0 NE2 D:HIS76 4.1 85.6 1.0 ND1 D:HIS6 4.2 75.2 1.0 NE2 D:HIS77 4.3 109.6 1.0 OD1 D:ASP8 4.5 79.0 1.0 CB D:ASP57 4.5 77.0 1.0 ND1 D:HIS76 4.5 83.9 1.0 CG D:ASP8 4.6 74.2 1.0 CE1 D:HIS6 4.6 75.0 1.0 CB D:ASP127 4.7 73.9 1.0 NZ D:LYS288 4.8 95.4 1.0 OD1 D:ASP10 4.9 67.3 1.0 C3' D:AMP401 4.9 98.9 1.0

Manganese binding site 2 out of 3 in the Pap Phosphatase From Methanothermococcus Thermolithotrophicus Refined to 3.1 A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Pap Phosphatase From Methanothermococcus Thermolithotrophicus Refined to 3.1 A within 5.0Å range: probe atom residue distance (Å) B Occ E:Mn403 b:93.5 occ:0.65 OD2 E:ASP57 2.6 89.4 1.0 OD1 E:ASP127 2.8 116.0 1.0 OD2 E:ASP10 3.0 99.9 1.0 OD1 E:ASP57 3.1 89.0 1.0 OD2 E:ASP127 3.1 98.4 1.0 CG E:ASP57 3.2 95.3 1.0 CG E:ASP127 3.3 101.0 1.0 OD2 E:ASP8 3.5 81.3 1.0 O3' E:AMP401 3.5 92.9 1.0 CB E:ASP10 3.6 87.3 1.0 CG E:ASP10 3.7 92.4 1.0 ND1 E:HIS6 3.7 79.6 1.0 CE1 E:HIS76 3.9 89.4 1.0 OD1 E:ASP8 4.0 82.6 1.0 CE1 E:HIS6 4.1 82.6 1.0 CG E:ASP8 4.2 79.8 1.0 CE1 E:HIS77 4.3 100.8 1.0 NE2 E:HIS76 4.6 95.6 1.0 NE2 E:HIS77 4.6 102.9 1.0 CB E:ASP57 4.7 81.8 1.0 CB E:ASP127 4.8 80.1 1.0 CG E:HIS6 4.8 80.7 1.0 CA E:ASP10 4.9 74.4 1.0 ND1 E:HIS76 5.0 87.4 1.0 C3' E:AMP401 5.0 89.7 1.0 OD1 E:ASP10 5.0 84.8 1.0

Manganese binding site 3 out of 3 in the Pap Phosphatase From Methanothermococcus Thermolithotrophicus Refined to 3.1 A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Pap Phosphatase From Methanothermococcus Thermolithotrophicus Refined to 3.1 A within 5.0Å range: probe atom residue distance (Å) B Occ F:Mn503 b:101.5 occ:0.69 OD1 F:ASP127 2.6 105.0 1.0 OD2 F:ASP57 2.9 74.6 1.0 OD2 F:ASP127 2.9 93.9 1.0 CG F:ASP127 3.1 93.7 1.0 OD2 F:ASP10 3.1 70.9 1.0 OD2 F:ASP8 3.3 72.5 1.0 O3' F:AMP502 3.3 95.0 1.0 OD1 F:ASP57 3.3 79.7 1.0 CG F:ASP57 3.5 75.6 1.0 CB F:ASP10 3.8 69.9 1.0 CE1 F:HIS76 3.8 80.8 1.0 CG F:ASP10 3.9 71.0 1.0 ND1 F:HIS6 3.9 73.9 1.0 CG F:ASP8 4.2 72.0 1.0 CE1 F:HIS77 4.2 89.0 1.0 CE1 F:HIS6 4.2 76.9 1.0 OD1 F:ASP8 4.2 74.9 1.0 NE2 F:HIS77 4.4 110.3 1.0 NE2 F:HIS76 4.4 80.0 1.0 CB F:ASP127 4.6 76.6 1.0 C3' F:AMP502 4.8 84.7 1.0 NZ F:LYS288 4.8 104.0 1.0 ND1 F:HIS76 5.0 78.9 1.0

M.Jespersen, T.Wagner. How A Methanogen Assimilates Sulfate: Structural and Functional Elucidation of the Complete Sulfate-Reduction Pathway. To Be Published.