Magnesium in PDB 1rqn: Phosphonoacetaldehyde Hydrolase Complexed with Magnesium

The structure of Phosphonoacetaldehyde Hydrolase Complexed with Magnesium, PDB code: 1rqn was solved by M.C.Morais, G.Zhang, W.Zhang, D.B.Olsen, D.Dunaway-Mariano, K.N.Allen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.34 / 2.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	210.130, 45.180, 63.640, 90.00, 105.10, 90.00
R / Rfree (%)	24.6 / 27.7

The binding sites of Magnesium atom in the Phosphonoacetaldehyde Hydrolase Complexed with Magnesium (pdb code 1rqn). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Phosphonoacetaldehyde Hydrolase Complexed with Magnesium, PDB code: 1rqn:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Phosphonoacetaldehyde Hydrolase Complexed with Magnesium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Phosphonoacetaldehyde Hydrolase Complexed with Magnesium within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:32.4 occ:1.00 OD2 A:ASP12 2.4 58.3 1.0 OD1 A:ASP186 2.4 54.4 1.0 O A:ALA14 2.6 54.1 1.0 CG A:ASP12 3.1 57.9 1.0 OD1 A:ASP12 3.2 59.2 1.0 CG A:ASP186 3.3 56.8 1.0 OD2 A:ASP186 3.5 56.1 1.0 C A:ALA14 3.7 54.0 1.0 OD2 A:ASP190 3.7 62.5 1.0 CG2 A:THR187 3.7 59.2 1.0 O A:HOH502 4.0 29.9 1.0 CB A:ALA14 4.1 57.3 1.0 CA A:ALA14 4.2 55.0 1.0 N A:ALA14 4.3 55.2 1.0 NH1 A:ARG160 4.4 47.3 1.0 CB A:ASP12 4.5 56.2 1.0 CG A:ASP190 4.6 59.4 1.0 OG1 A:THR187 4.6 58.2 1.0 OD1 A:ASP190 4.6 59.0 1.0 OG1 A:THR16 4.6 55.3 1.0 CB A:ASP186 4.7 58.0 1.0 N A:GLY15 4.8 53.2 1.0 CB A:THR187 4.8 59.8 1.0 N A:ASP186 4.9 60.8 1.0

Magnesium binding site 2 out of 2 in the Phosphonoacetaldehyde Hydrolase Complexed with Magnesium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Phosphonoacetaldehyde Hydrolase Complexed with Magnesium within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg502 b:32.9 occ:1.00 O B:ALA14 2.5 47.6 1.0 OD2 B:ASP12 2.5 45.5 1.0 OD1 B:ASP186 2.7 39.8 1.0 CG B:ASP12 3.4 44.9 1.0 O B:HOH503 3.4 31.1 1.0 OD1 B:ASP12 3.5 46.7 1.0 C B:ALA14 3.5 47.3 1.0 CG B:ASP186 3.5 38.9 1.0 OD2 B:ASP186 3.6 37.9 1.0 CB B:ALA14 3.9 46.0 1.0 CA B:ALA14 4.1 45.8 1.0 OD2 B:ASP190 4.1 36.7 1.0 CG2 B:THR187 4.2 36.3 1.0 N B:ALA14 4.2 45.2 1.0 SG B:CYS22 4.3 47.3 1.0 N B:GLY15 4.6 47.6 1.0 NH1 B:ARG160 4.6 36.7 1.0 CA B:GLY50 4.6 42.6 1.0 CB B:ASP12 4.8 42.8 1.0 OG1 B:THR16 4.8 49.0 1.0 CG B:MET49 4.8 43.0 1.0 N B:GLY50 4.9 41.5 1.0 C B:TRP13 5.0 45.1 1.0 CA B:GLY15 5.0 48.3 1.0 CB B:ASP186 5.0 39.1 1.0

M.C.Morais, G.Zhang, W.Zhang, D.B.Olsen, D.Dunaway-Mariano, K.N.Allen. X-Ray Crystallographic and Site-Directed Mutagenesis Analysis of the Mechanism of Schiff-Base Formation in Phosphonoacetaldehyde Hydrolase Catalysis J.Biol.Chem. V. 279 9353 2004.
ISSN: ISSN 0021-9258
PubMed: 14670958
DOI: 10.1074/JBC.M312345200