Manganese in PDB 2jfr: Crystal Structure of the Ppm Ser-Thr Phosphatase Mspp From Mycobacterium Smegmatis in Complex with Phosphate at 0.83 A Resolution

The structure of Crystal Structure of the Ppm Ser-Thr Phosphatase Mspp From Mycobacterium Smegmatis in Complex with Phosphate at 0.83 A Resolution, PDB code: 2jfr was solved by M.Bellinzoni, A.Wehenkel, W.Shepard, P.M.Alzari, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 0.83
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	76.382, 83.998, 33.478, 90.00, 90.00, 90.00
R / Rfree (%)	9.5 / 12.4

The structure of Crystal Structure of the Ppm Ser-Thr Phosphatase Mspp From Mycobacterium Smegmatis in Complex with Phosphate at 0.83 A Resolution also contains other interesting chemical elements:

Magnesium	(Mg)	4 atoms
Chlorine	(Cl)	1 atom

The binding sites of Manganese atom in the Crystal Structure of the Ppm Ser-Thr Phosphatase Mspp From Mycobacterium Smegmatis in Complex with Phosphate at 0.83 A Resolution (pdb code 2jfr). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of the Ppm Ser-Thr Phosphatase Mspp From Mycobacterium Smegmatis in Complex with Phosphate at 0.83 A Resolution, PDB code: 2jfr:

Manganese binding site 1 out of 1 in the Crystal Structure of the Ppm Ser-Thr Phosphatase Mspp From Mycobacterium Smegmatis in Complex with Phosphate at 0.83 A Resolution


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 Ppm Ser-Thr Phosphatase Mspp From Mycobacterium Smegmatis in Complex with Phosphate at 0.83 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1235 b:13.8 occ:0.56 OD1 A:ASP185 2.0 20.9 0.4 OD1 A:ASP185 2.1 13.2 0.6 O A:HOH2488 2.1 17.9 0.8 OD2 A:ASP35 2.1 14.1 1.0 O A:HOH2485 2.1 14.2 1.0 OD2 A:ASP223 2.1 15.6 1.0 O A:HOH2486 2.2 14.6 0.8 O3 A:PO41239 2.3 20.9 0.2 O1 A:PO41239 2.3 19.6 0.2 P A:PO41239 2.9 18.0 0.2 CG A:ASP35 3.0 13.2 1.0 CG A:ASP185 3.1 15.5 0.6 CG A:ASP223 3.1 15.3 1.0 CG A:ASP185 3.1 14.5 0.4 OD1 A:ASP223 3.4 15.8 1.0 OD1 A:ASP35 3.4 13.8 1.0 OD2 A:ASP185 3.5 16.0 0.4 OD2 A:ASP185 3.5 16.9 0.6 MG A:MG1236 3.6 15.6 0.4 MG A:MG1234 3.7 13.9 1.0 O A:HOH2489 3.9 22.5 0.8 O A:HOH2487 3.9 14.6 0.8 O4 A:PO41239 3.9 19.4 0.2 O2 A:PO41239 4.0 24.8 0.2 O A:HOH2287 4.1 18.9 1.0 O A:HOH2289 4.2 14.7 1.0 O A:HOH2410 4.2 29.1 1.0 N A:GLY186 4.3 14.7 1.0 O A:HOH2411 4.3 18.4 0.4 OD1 A:ASP22 4.3 14.4 1.0 O A:HOH2131 4.4 14.2 1.0 CB A:ASP185 4.4 15.4 0.6 CB A:ASP35 4.4 13.6 1.0 CB A:ASP223 4.4 15.4 1.0 CB A:ASP185 4.4 14.4 0.4 O A:ASN224 4.5 14.3 1.0 N A:ASP185 4.5 14.5 1.0 C A:ASP185 4.7 15.0 1.0 CA A:ASP185 4.7 14.7 0.6 CB A:SER184 4.8 13.9 1.0 CA A:ASP185 4.8 14.7 0.4 O A:HOH2493 4.9 51.4 1.0 CA A:GLY186 5.0 15.0 1.0 OG A:SER184 5.0 14.5 1.0

M.Bellinzoni, A.Wehenkel, W.Shepard, P.M.Alzari. Insights Into the Mechanism of Ppm Ser/Thr Phosphatases From the Atomic Resolution Structures of A Mycobacterial Enzyme Structure V. 15 863 2007.
ISSN: ISSN 0969-2126
PubMed: 17637345
DOI: 10.1016/J.STR.2007.06.002