Magnesium in PDB 1vr0: Crystal Structure of Putative 2-Phosphosulfolactate Phosphatase (15026306) From Clostridium Acetobutylicum at 2.6 A Resolution

All present enzymatic activity of Crystal Structure of Putative 2-Phosphosulfolactate Phosphatase (15026306) From Clostridium Acetobutylicum at 2.6 A Resolution:
3.1.3.71;

The structure of Crystal Structure of Putative 2-Phosphosulfolactate Phosphatase (15026306) From Clostridium Acetobutylicum at 2.6 A Resolution, PDB code: 1vr0 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)	38.70 / 2.49
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	46.686, 69.193, 453.518, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 22.9

The binding sites of Magnesium atom in the Crystal Structure of Putative 2-Phosphosulfolactate Phosphatase (15026306) From Clostridium Acetobutylicum at 2.6 A Resolution (pdb code 1vr0). 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 Putative 2-Phosphosulfolactate Phosphatase (15026306) From Clostridium Acetobutylicum at 2.6 A Resolution, PDB code: 1vr0:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Putative 2-Phosphosulfolactate Phosphatase (15026306) From Clostridium Acetobutylicum at 2.6 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 Putative 2-Phosphosulfolactate Phosphatase (15026306) From Clostridium Acetobutylicum at 2.6 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg400 b:36.0 occ:1.00 OD1 A:ASP26 2.2 47.6 1.0 OD2 A:ASP155 2.4 38.7 1.0 O A:HOH452 2.5 45.2 1.0 O A:GLY146 2.5 40.8 1.0 O A:HOH411 2.5 26.1 1.0 O A:HOH406 3.0 18.5 1.0 CG A:ASP155 3.3 40.1 1.0 CG A:ASP26 3.4 42.5 1.0 C A:GLY146 3.4 40.1 1.0 OD1 A:ASP155 3.5 42.5 1.0 N A:GLY146 3.9 39.6 1.0 CA A:ASP26 4.0 41.4 1.0 CA A:GLY146 4.1 39.7 1.0 OD2 A:ASP154 4.1 47.3 1.0 CB A:ASP26 4.2 40.6 1.0 OD2 A:ASP26 4.2 45.1 1.0 CB A:ALA145 4.3 38.4 1.0 ND2 A:ASN104 4.3 40.9 1.0 CB A:ASN104 4.4 43.5 1.0 N A:THR147 4.4 40.0 1.0 C A:ALA145 4.5 39.2 1.0 C A:ASP26 4.5 41.6 1.0 OD1 A:ASP154 4.6 45.2 1.0 O A:LEU28 4.6 40.1 1.0 CB A:ASP155 4.7 40.3 1.0 CG A:ASN104 4.7 43.4 1.0 CA A:THR147 4.7 40.6 1.0 CG A:ASP154 4.7 42.2 1.0 CB A:THR147 4.7 41.0 1.0 N A:MSE27 4.8 41.7 1.0 O A:ILE25 4.9 40.6 1.0 CA A:ALA145 4.9 39.2 1.0 CB A:SER152 5.0 38.3 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Putative 2-Phosphosulfolactate Phosphatase (15026306) From Clostridium Acetobutylicum at 2.6 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 Putative 2-Phosphosulfolactate Phosphatase (15026306) From Clostridium Acetobutylicum at 2.6 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg400 b:41.4 occ:1.00 OD1 B:ASP26 2.2 48.8 1.0 O B:HOH423 2.3 52.0 1.0 OD2 B:ASP155 2.4 39.4 1.0 O B:HOH404 2.6 21.5 1.0 O B:GLY146 2.6 40.6 1.0 O B:HOH412 3.1 24.1 1.0 CG B:ASP155 3.2 40.4 1.0 OD1 B:ASP155 3.3 38.6 1.0 CG B:ASP26 3.4 42.5 1.0 C B:GLY146 3.5 39.9 1.0 N B:GLY146 4.0 39.2 1.0 CA B:ASP26 4.0 41.4 1.0 OD2 B:ASP154 4.1 44.4 1.0 CA B:GLY146 4.1 39.5 1.0 CB B:ASP26 4.2 41.5 1.0 OD2 B:ASP26 4.3 44.7 1.0 CB B:ALA145 4.3 39.6 1.0 OD1 B:ASP154 4.4 41.7 1.0 N B:THR147 4.4 40.3 1.0 CB B:ASN104 4.5 43.1 1.0 C B:ASP26 4.5 41.7 1.0 CB B:ASP155 4.6 40.3 1.0 O B:LEU28 4.6 40.3 1.0 ND2 B:ASN104 4.6 39.0 1.0 CG B:ASP154 4.6 41.2 1.0 OG1 B:THR147 4.6 43.8 1.0 C B:ALA145 4.6 39.1 1.0 N B:MSE27 4.7 41.7 1.0 CG B:ASN104 4.8 42.0 1.0 O B:ILE25 4.8 40.8 1.0 CB B:SER152 4.9 38.3 1.0 OG B:SER152 4.9 38.7 1.0 CA B:THR147 4.9 40.7 1.0 CA B:ALA145 5.0 39.3 1.0

M.Didonato, S.S.Krishna, R.Schwarzenbacher, D.Mcmullan, S.Agarwalla, S.M.Brittain, M.D.Miller, P.Abdubek, E.Ambing, H.L.Axelrod, J.M.Canaves, H.J.Chiu, A.M.Deacon, L.Duan, M.A.Elsliger, A.Godzik, S.K.Grzechnik, J.Hale, E.Hampton, J.Haugen, L.Jaroszewski, K.K.Jin, H.E.Klock, M.W.Knuth, E.Koesema, A.Kreusch, P.Kuhn, S.A.Lesley, I.Levin, A.T.Morse, E.Nigoghossian, L.Okach, S.Oommachen, J.Paulsen, K.Quijano, R.Reyes, C.L.Rife, G.Spraggon, R.C.Stevens, H.Van Den Bedem, A.White, G.Wolf, Q.Xu, K.O.Hodgson, J.Wooley, I.A.Wilson. Crystal Structure of 2-Phosphosulfolactate Phosphatase (Comb) From Clostridium Acetobutylicum at 2.6 A Resolution Reveals A New Fold with A Novel Active Site. Proteins V. 65 771 2006.
ISSN: ISSN 0887-3585
PubMed: 16927339
DOI: 10.1002/PROT.20978