Magnesium in PDB 2fea: Crystal Structure of Mtnx Phosphatase From Bacillus Subtilis at 2.00 A Resolution

The structure of Crystal Structure of Mtnx Phosphatase From Bacillus Subtilis at 2.00 A Resolution, PDB code: 2fea was solved by Joint Center For Structural Genomics (Jcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.95 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	59.013, 43.104, 109.553, 90.00, 98.91, 90.00
R / Rfree (%)	16 / 21.7

The structure of Crystal Structure of Mtnx Phosphatase From Bacillus Subtilis at 2.00 A Resolution also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Magnesium atom in the Crystal Structure of Mtnx Phosphatase From Bacillus Subtilis at 2.00 A Resolution (pdb code 2fea). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Mtnx Phosphatase From Bacillus Subtilis at 2.00 A Resolution, PDB code: 2fea:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Mtnx Phosphatase From Bacillus Subtilis at 2.00 A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Mtnx Phosphatase From Bacillus Subtilis at 2.00 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1301 b:44.5 occ:1.00 O A:ASP13 2.2 38.5 1.0 OD1 A:ASP170 2.3 41.2 1.0 OD2 A:ASP11 2.3 37.5 1.0 O A:HOH1453 2.5 54.1 1.0 OG A:SER171 2.6 42.4 1.0 CG A:ASP170 3.1 41.9 1.0 OD2 A:ASP170 3.2 40.8 1.0 C A:ASP13 3.4 40.0 1.0 CG A:ASP11 3.4 36.0 1.0 O A:HOH1312 3.8 26.6 1.0 CB A:SER171 4.0 39.2 1.0 OD1 A:ASP11 4.1 42.1 1.0 OG1 A:THR15 4.2 42.9 1.0 CB A:ASP13 4.3 40.6 1.0 N A:SER171 4.3 36.5 1.0 N A:GLY14 4.3 37.3 1.0 CA A:GLY14 4.3 40.6 1.0 CA A:ASP13 4.3 38.3 1.0 CB A:ASP11 4.4 33.1 1.0 CB A:ASP170 4.5 34.4 1.0 N A:ASP13 4.5 38.6 1.0 C A:GLY14 4.6 41.6 1.0 O A:HOH1313 4.6 26.5 1.0 N A:THR15 4.6 38.7 1.0 CA A:SER171 4.6 34.6 1.0 O A:HOH1347 4.8 37.1 1.0 N A:ASP170 4.8 35.1 1.0 C A:ASP170 4.8 36.5 1.0 CA A:ASP170 4.9 35.8 1.0 C A:PHE12 5.0 35.5 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Mtnx Phosphatase From Bacillus Subtilis at 2.00 A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Mtnx Phosphatase From Bacillus Subtilis at 2.00 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg2301 b:42.6 occ:1.00 O B:HOH2354 2.2 39.2 1.0 O B:ASP13 2.2 36.5 1.0 OD2 B:ASP11 2.3 39.5 1.0 OD1 B:ASP170 2.4 38.0 1.0 O B:HOH2322 2.5 30.0 1.0 CG B:ASP170 3.3 41.4 1.0 OD2 B:ASP170 3.4 40.1 1.0 CG B:ASP11 3.4 35.6 1.0 C B:ASP13 3.4 36.4 1.0 O B:HOH2311 3.6 23.9 1.0 CB B:SER171 3.7 39.2 1.0 O B:HOH2462 3.8 53.9 1.0 O B:HOH2334 3.8 35.8 1.0 OD1 B:ASP11 4.1 38.0 1.0 CA B:GLY14 4.2 35.8 1.0 N B:GLY14 4.2 35.4 1.0 N B:SER171 4.3 35.7 1.0 O B:HOH2343 4.4 37.6 1.0 OG1 B:THR15 4.4 32.7 1.0 O B:HOH2336 4.4 35.3 1.0 CA B:ASP13 4.5 37.0 1.0 CB B:ASP11 4.5 31.1 1.0 N B:THR15 4.5 37.5 1.0 C B:GLY14 4.5 34.2 1.0 CA B:SER171 4.6 37.2 1.0 CB B:ASP170 4.7 32.6 1.0 N B:ASP13 4.7 38.1 1.0 CB B:ASP13 4.8 39.8 1.0 OG B:SER171 4.8 45.0 1.0 O B:HOH2466 4.8 54.1 1.0

Q.Xu, K.S.Saikatendu, S.S.Krishna, D.Mcmullan, P.Abdubek, S.Agarwalla, E.Ambing, T.Astakhova, H.L.Axelrod, D.Carlton, H.J.Chiu, T.Clayton, M.Didonato, L.Duan, M.A.Elsliger, J.Feuerhelm, S.K.Grzechnik, J.Hale, E.Hampton, G.W.Han, J.Haugen, L.Jaroszewski, K.K.Jin, H.E.Klock, M.W.Knuth, E.Koesema, M.D.Miller, A.T.Morse, E.Nigoghossian, L.Okach, S.Oommachen, J.Paulsen, R.Reyes, C.L.Rife, R.Schwarzenbacher, H.Van Den Bedem, A.White, G.Wolf, K.O.Hodgson, J.Wooley, A.M.Deacon, A.Godzik, S.A.Lesley, I.A.Wilson. Crystal Structure of Mtnx Phosphatase From Bacillus Subtilis at 2.0 A Resolution Provides A Structural Basis For Bipartite Phosphomonoester Hydrolysis of 2-Hydroxy-3-Keto-5-Methylthiopentenyl-1-Phosphate. Proteins V. 69 433 2007.
ISSN: ISSN 0887-3585
PubMed: 17654724
DOI: 10.1002/PROT.21602