Magnesium in PDB 2x4d: Crystal Structure of Human Phospholysine Phosphohistidine Inorganic Pyrophosphate Phosphatase Lhpp

All present enzymatic activity of Crystal Structure of Human Phospholysine Phosphohistidine Inorganic Pyrophosphate Phosphatase Lhpp:
3.6.1.1;

The structure of Crystal Structure of Human Phospholysine Phosphohistidine Inorganic Pyrophosphate Phosphatase Lhpp, PDB code: 2x4d was solved by M.Vollmar, C.Gileadi, K.Guo, P.Savitsky, J.R.C.Muniz, W.Yue, C.Allerston, F.Von Delft, C.Bountra, C.H.Arrowsmith, J.Weigelt, A.Edwards, K.L.Kavanagh, U.Oppermann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 1.92
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	59.210, 39.410, 112.920, 90.00, 91.79, 90.00
R / Rfree (%)	22.7 / 25.8

The binding sites of Magnesium atom in the Crystal Structure of Human Phospholysine Phosphohistidine Inorganic Pyrophosphate Phosphatase Lhpp (pdb code 2x4d). 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 Human Phospholysine Phosphohistidine Inorganic Pyrophosphate Phosphatase Lhpp, PDB code: 2x4d:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Human Phospholysine Phosphohistidine Inorganic Pyrophosphate Phosphatase Lhpp


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 Human Phospholysine Phosphohistidine Inorganic Pyrophosphate Phosphatase Lhpp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:9.5 occ:1.00 OD1 A:ASP214 2.2 11.9 1.0 O A:HOH2139 2.2 10.0 1.0 OD2 A:ASP17 2.2 15.0 1.0 O A:POP500 2.2 25.9 1.0 O A:SER19 2.4 9.9 1.0 O A:HOH2183 2.6 16.6 1.0 OD1 A:ASP17 2.8 17.2 1.0 CG A:ASP17 2.9 11.8 1.0 CG A:ASP214 3.2 9.1 1.0 C A:SER19 3.5 10.0 1.0 OD2 A:ASP214 3.7 9.0 1.0 P1 A:POP500 3.7 26.9 1.0 OD2 A:ASP219 3.9 11.8 1.0 O2 A:POP500 4.1 23.8 1.0 O A:HOH2184 4.2 15.1 1.0 CE A:LYS237 4.2 10.6 1.0 O3 A:POP500 4.3 18.8 1.0 CA A:SER19 4.3 9.9 1.0 CB A:SER19 4.3 11.1 1.0 CB A:ASP17 4.3 11.8 1.0 O A:HOH2134 4.3 5.4 1.0 N A:SER19 4.3 10.5 1.0 N A:ASP214 4.4 8.9 1.0 CB A:ASP214 4.4 9.4 1.0 N A:GLY20 4.5 8.4 1.0 O A:HOH2182 4.6 16.4 1.0 NZ A:LYS237 4.6 10.1 1.0 O A:HOH2147 4.6 17.3 1.0 CA A:GLY20 4.7 9.2 1.0 CA A:ASP214 4.8 9.8 1.0 O1 A:POP500 4.9 28.7 1.0 CG A:ASP219 4.9 10.4 1.0 N A:ASP215 5.0 9.8 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Human Phospholysine Phosphohistidine Inorganic Pyrophosphate Phosphatase Lhpp


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 Human Phospholysine Phosphohistidine Inorganic Pyrophosphate Phosphatase Lhpp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg501 b:27.9 occ:1.00 O B:HOH2026 2.0 10.1 1.0 O B:SER19 2.1 10.1 1.0 OD2 B:ASP17 2.2 15.4 1.0 O B:POP500 2.3 34.1 1.0 OD1 B:ASP214 2.3 11.1 1.0 CG B:ASP17 2.9 11.6 1.0 OD1 B:ASP17 2.9 16.2 1.0 CG B:ASP214 3.3 9.9 1.0 C B:SER19 3.3 10.0 1.0 OD2 B:ASP214 3.7 9.7 1.0 P1 B:POP500 3.7 35.4 1.0 O2 B:POP500 4.0 28.9 1.0 O B:HOH2024 4.0 18.6 1.0 CA B:SER19 4.1 10.3 1.0 CB B:SER19 4.1 10.6 1.0 OD2 B:ASP219 4.1 11.7 1.0 O3 B:POP500 4.1 30.6 1.0 N B:SER19 4.2 10.0 1.0 CE B:LYS237 4.3 11.0 1.0 N B:GLY20 4.3 9.2 1.0 CB B:ASP17 4.4 11.1 1.0 CB B:ASP214 4.5 9.8 1.0 CA B:GLY20 4.6 9.1 1.0 N B:ASP214 4.6 9.3 1.0 NZ B:LYS237 4.8 11.2 1.0 O1 B:POP500 4.9 34.2 1.0 C B:ILE18 4.9 9.4 1.0 CA B:ASP214 5.0 9.7 1.0 N B:ILE18 5.0 9.9 1.0

M.Vollmar, C.Gileadi, K.Guo, P.Savitsky, J.R.C.Muniz, W.Yue, C.Allerston, F.Von Delft, C.Bountra, C.H.Arrowsmith, J.Weigelt, A.Edwards, K.L.Kavanagh, U.Oppermann. Crystal Structure of Human Phospholysine Phosphohistidine Inorganic Pyrophosphate Phosphatase Lhpp To Be Published.