Manganese in PDB 2jfs: Crystal Structure of the Ppm Ser-Thr Phosphatase Mspp From Mycobacterium Smegmatis in Complex with Cacodylate

The structure of Crystal Structure of the Ppm Ser-Thr Phosphatase Mspp From Mycobacterium Smegmatis in Complex with Cacodylate, PDB code: 2jfs 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)	25.38 / 1.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	36.568, 65.786, 110.059, 90.00, 90.00, 90.00
R / Rfree (%)	17.8 / 19.1

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

Arsenic

(As)

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 Cacodylate (pdb code 2jfs). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the Crystal Structure of the Ppm Ser-Thr Phosphatase Mspp From Mycobacterium Smegmatis in Complex with Cacodylate, PDB code: 2jfs:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in the Crystal Structure of the Ppm Ser-Thr Phosphatase Mspp From Mycobacterium Smegmatis in Complex with Cacodylate


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 Cacodylate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1234 b:10.5 occ:0.75 O2 A:CAC1237 2.1 9.3 0.6 OD1 A:ASP35 2.1 14.7 1.0 O A:GLY36 2.2 13.9 1.0 O A:HOH2231 2.2 10.4 1.0 O A:HOH2230 2.3 10.8 1.0 O A:HOH2229 2.3 14.4 1.0 CG A:ASP35 3.2 13.5 1.0 C A:GLY36 3.4 13.2 1.0 AS A:CAC1237 3.4 13.2 0.6 MN A:MN1235 3.8 9.7 1.0 OD2 A:ASP35 3.8 14.2 1.0 O A:HOH2236 3.9 21.4 1.0 N A:GLY36 3.9 13.0 1.0 O1 A:CAC1237 4.0 7.5 0.6 O A:HOH2023 4.0 18.7 1.0 C A:ASP35 4.0 12.9 1.0 OD1 A:ASP22 4.2 13.6 1.0 CA A:GLY36 4.2 13.0 1.0 O A:HOH2232 4.3 10.2 1.0 CB A:GLN21 4.3 13.1 1.0 N A:PHE37 4.3 13.4 1.0 C2 A:CAC1237 4.3 14.8 0.6 OE1 A:GLN21 4.4 16.3 1.0 CA A:PHE37 4.4 13.5 1.0 CB A:ASP35 4.4 13.3 1.0 O A:ASP35 4.4 12.9 1.0 CA A:ASP35 4.5 12.4 1.0 OD1 A:ASP223 4.6 15.1 1.0 OD1 A:ASN224 4.6 13.0 1.0 O A:HOH2226 4.6 20.4 1.0 CB A:PHE37 4.7 14.7 1.0 O A:GLN21 4.9 13.2 1.0 C A:GLN21 4.9 13.5 1.0 NH1 A:ARG17 4.9 21.9 0.5 C1 A:CAC1237 4.9 9.8 0.6

Manganese binding site 2 out of 3 in the Crystal Structure of the Ppm Ser-Thr Phosphatase Mspp From Mycobacterium Smegmatis in Complex with Cacodylate


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 Ppm Ser-Thr Phosphatase Mspp From Mycobacterium Smegmatis in Complex with Cacodylate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1235 b:9.7 occ:1.00 OD1 A:ASP185 2.1 14.0 1.0 OD2 A:ASP35 2.2 14.2 1.0 O A:HOH2232 2.2 10.2 1.0 O1 A:CAC1237 2.2 7.5 0.6 OD2 A:ASP223 2.3 14.6 1.0 O A:HOH2230 2.3 10.8 1.0 CG A:ASP35 3.1 13.5 1.0 CG A:ASP185 3.2 17.0 1.0 CG A:ASP223 3.2 14.2 1.0 OD1 A:ASP35 3.3 14.7 1.0 O A:HOH2234 3.4 21.9 1.0 OD1 A:ASP223 3.4 15.1 1.0 AS A:CAC1237 3.5 13.2 0.6 OD2 A:ASP185 3.6 16.4 1.0 MN A:MN1236 3.7 7.5 0.5 MN A:MN1234 3.8 10.5 0.8 O2 A:CAC1237 3.9 9.3 0.6 O A:HOH2023 4.1 18.7 1.0 O A:HOH2043 4.2 10.1 1.0 N A:GLY186 4.3 13.6 1.0 C2 A:CAC1237 4.4 14.8 0.6 O A:HOH2231 4.4 10.4 1.0 OD1 A:ASP22 4.4 13.6 1.0 CB A:ASP35 4.5 13.3 1.0 N A:ASP185 4.5 14.0 1.0 CB A:ASP185 4.5 14.1 1.0 CB A:ASP223 4.6 14.9 1.0 O A:HOH2224 4.6 20.5 1.0 O A:ASN224 4.6 13.2 1.0 O A:HOH2235 4.8 23.3 1.0 C A:ASP185 4.8 14.6 1.0 CA A:ASP185 4.8 14.2 1.0 CB A:SER184 4.8 14.3 1.0 CA A:GLY186 4.9 13.8 1.0

Manganese binding site 3 out of 3 in the Crystal Structure of the Ppm Ser-Thr Phosphatase Mspp From Mycobacterium Smegmatis in Complex with Cacodylate


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 Ppm Ser-Thr Phosphatase Mspp From Mycobacterium Smegmatis in Complex with Cacodylate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1236 b:7.5 occ:0.50 OD2 A:ASP185 2.1 16.4 1.0 O1 A:CAC1237 2.1 7.5 0.6 ND1 A:HIS153 2.2 20.4 1.0 O A:HOH2235 2.2 23.3 1.0 O A:HOH2234 2.3 21.9 1.0 O A:HOH2233 2.3 13.6 1.0 CE1 A:HIS153 3.0 25.1 1.0 CG A:ASP185 3.1 17.0 1.0 CG A:HIS153 3.3 21.7 1.0 OD1 A:ASP185 3.4 14.0 1.0 AS A:CAC1237 3.5 13.2 0.6 MN A:MN1235 3.7 9.7 1.0 CB A:HIS153 3.7 18.3 1.0 C1 A:CAC1237 3.8 9.8 0.6 O A:HOH2023 4.1 18.7 1.0 OD2 A:ASP223 4.1 14.6 1.0 OD2 A:ASP111 4.1 18.6 1.0 O A:HOH2224 4.2 20.5 1.0 NE2 A:HIS153 4.2 24.7 1.0 CD2 A:HIS153 4.4 23.7 1.0 CB A:ASP185 4.4 14.1 1.0 CA A:HIS153 4.4 19.4 1.0 O A:HOH2167 4.5 33.0 1.0 C2 A:CAC1237 4.5 14.8 0.6 O A:HIS153 4.6 21.9 1.0 O A:HOH2112 4.7 25.5 1.0 O A:HOH2230 4.7 10.8 1.0 OD2 A:ASP35 4.8 14.2 1.0 O2 A:CAC1237 4.8 9.3 0.6

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