Manganese in PDB 2cm1: Crystal Structure of the Catalytic Domain of Serine Threonine Protein Phosphatase Pstp in Complex with 2 Manganese Ions.

All present enzymatic activity of Crystal Structure of the Catalytic Domain of Serine Threonine Protein Phosphatase Pstp in Complex with 2 Manganese Ions.:
3.1.3.16;

The structure of Crystal Structure of the Catalytic Domain of Serine Threonine Protein Phosphatase Pstp in Complex with 2 Manganese Ions., PDB code: 2cm1 was solved by A.Wehenkel, A.Villarino, M.Bellinzoni, P.M.Alzari, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	59.87 / 2.0
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	69.142, 69.142, 89.431, 90.00, 90.00, 120.00
R / Rfree (%)	19.7 / 24.3

The binding sites of Manganese atom in the Crystal Structure of the Catalytic Domain of Serine Threonine Protein Phosphatase Pstp in Complex with 2 Manganese Ions. (pdb code 2cm1). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of the Catalytic Domain of Serine Threonine Protein Phosphatase Pstp in Complex with 2 Manganese Ions., PDB code: 2cm1:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of the Catalytic Domain of Serine Threonine Protein Phosphatase Pstp in Complex with 2 Manganese Ions.


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 Catalytic Domain of Serine Threonine Protein Phosphatase Pstp in Complex with 2 Manganese Ions. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn301 b:19.1 occ:1.00 OD2 A:ASP229 2.1 18.9 1.0 OD1 A:ASP191 2.1 18.8 1.0 O A:HOH2138 2.1 24.0 1.0 O A:HOH2137 2.1 14.9 1.0 OD2 A:ASP38 2.2 19.6 1.0 O A:HOH2136 2.2 17.4 1.0 CG A:ASP38 3.1 18.5 1.0 CG A:ASP191 3.1 18.8 1.0 CG A:ASP229 3.1 19.7 1.0 OD1 A:ASP38 3.3 19.7 1.0 OD2 A:ASP191 3.4 25.5 1.0 OD1 A:ASP229 3.5 18.0 1.0 MN A:MN302 3.9 27.8 0.7 O A:HOH2141 4.0 25.6 1.0 O A:HOH2022 4.0 15.0 1.0 O A:HOH2139 4.1 19.9 1.0 N A:GLY192 4.3 16.4 1.0 O A:HOH2115 4.3 32.4 1.0 O A:HOH2059 4.3 23.3 1.0 CB A:ASP38 4.4 14.9 1.0 O A:ASN230 4.4 17.1 1.0 OD1 A:ASP25 4.4 18.6 1.0 CB A:ASP191 4.4 15.3 1.0 CB A:ASP229 4.5 17.3 1.0 N A:ASP191 4.5 15.3 1.0 CB A:SER190 4.7 12.4 1.0 C A:ASP191 4.7 15.9 1.0 CA A:ASP191 4.7 15.0 1.0 OG A:SER190 5.0 12.6 1.0 CA A:GLY192 5.0 15.8 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of the Catalytic Domain of Serine Threonine Protein Phosphatase Pstp in Complex with 2 Manganese Ions.


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 Catalytic Domain of Serine Threonine Protein Phosphatase Pstp in Complex with 2 Manganese Ions. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn302 b:27.8 occ:0.70 OD1 A:ASP38 2.1 19.7 1.0 O A:GLY39 2.2 22.9 1.0 O A:HOH2141 2.2 25.6 1.0 O A:HOH2136 2.4 17.4 1.0 O A:HOH2140 2.4 25.9 1.0 O A:HOH2139 2.5 19.9 1.0 CG A:ASP38 3.3 18.5 1.0 C A:GLY39 3.3 22.5 1.0 OD2 A:ASP38 3.8 19.6 1.0 MN A:MN301 3.9 19.1 1.0 N A:GLY39 3.9 18.1 1.0 O A:HOH2021 4.0 18.7 1.0 O A:HOH2138 4.0 24.0 1.0 C A:ASP38 4.1 17.0 1.0 OE1 A:GLU24 4.1 35.9 1.0 N A:MET40 4.2 25.5 1.0 CA A:GLY39 4.2 20.1 1.0 CB A:GLU24 4.3 16.7 1.0 CA A:MET40 4.4 30.4 1.0 CB A:MET40 4.4 29.6 1.0 O A:ASP38 4.4 17.4 1.0 CB A:ASP38 4.5 14.9 1.0 OD1 A:ASP25 4.6 18.6 1.0 O A:HOH2137 4.6 14.9 1.0 CA A:ASP38 4.6 16.1 1.0 OD1 A:ASN230 4.7 18.2 1.0 NH1 A:ARG20 4.7 32.0 1.0 OD1 A:ASP229 4.8 18.0 1.0 O A:GLU24 4.9 14.2 1.0 O A:HOH2059 5.0 23.3 1.0 O A:HOH2135 5.0 21.4 1.0

A.Wehenkel, M.Bellinzoni, F.Schaeffer, A.Villarino, P.M.Alzari. Structural and Binding Studies of the Three-Metal Center in Two Mycobacterial Ppm Ser/Thr Protein Phosphatases. J.Mol.Biol. V. 374 890 2007.
ISSN: ISSN 0022-2836
PubMed: 17961594
DOI: 10.1016/J.JMB.2007.09.076