Magnesium in PDB 2gqr: Saicar Synthetase Complexed with Adp-MG2+

All present enzymatic activity of Saicar Synthetase Complexed with Adp-MG2+:
6.3.2.6;

The structure of Saicar Synthetase Complexed with Adp-MG2+, PDB code: 2gqr was solved by N.D.Ginder, R.B.Honzatko, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.93 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.290, 67.160, 148.780, 90.00, 90.00, 90.00
R / Rfree (%)	20.4 / 23.9

The binding sites of Magnesium atom in the Saicar Synthetase Complexed with Adp-MG2+ (pdb code 2gqr). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Saicar Synthetase Complexed with Adp-MG2+, PDB code: 2gqr:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Saicar Synthetase Complexed with Adp-MG2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Saicar Synthetase Complexed with Adp-MG2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg239 b:20.2 occ:1.00 O2A A:ADP238 2.0 24.3 1.0 O A:HOH243 2.1 9.7 1.0 O A:HOH240 2.1 21.1 1.0 O3B A:ADP238 2.1 23.3 1.0 O A:HOH241 2.1 13.2 1.0 O A:HOH242 2.2 14.7 1.0 PA A:ADP238 3.2 18.4 1.0 PB A:ADP238 3.3 20.9 1.0 O3A A:ADP238 3.4 21.2 1.0 NZ A:LYS13 3.8 15.6 1.0 OD1 A:ASP191 4.0 16.6 1.0 OD2 A:ASP191 4.1 15.4 1.0 OE1 A:GLU179 4.2 17.7 1.0 O2B A:ADP238 4.2 27.5 1.0 NZ A:LYS177 4.2 21.8 1.0 O A:HOH287 4.2 22.7 1.0 O A:HOH261 4.3 23.3 1.0 O1A A:ADP238 4.3 21.6 1.0 O5' A:ADP238 4.3 23.7 1.0 NZ A:LYS123 4.4 17.6 1.0 O1B A:ADP238 4.4 23.9 1.0 CG A:ASP191 4.5 16.2 1.0 O A:HOH393 4.6 45.2 1.0 O A:HOH403 4.6 36.6 1.0 OE1 A:GLU192 4.9 22.3 1.0 C5' A:ADP238 5.0 21.7 1.0

Magnesium binding site 2 out of 2 in the Saicar Synthetase Complexed with Adp-MG2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Saicar Synthetase Complexed with Adp-MG2+ within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg239 b:22.6 occ:1.00 O3B B:ADP238 2.0 31.4 1.0 O B:HOH243 2.1 19.6 1.0 O B:HOH240 2.1 23.7 1.0 O2A B:ADP238 2.2 31.8 1.0 O B:HOH241 2.2 18.5 1.0 O B:HOH242 2.2 23.2 1.0 PB B:ADP238 3.1 27.9 1.0 PA B:ADP238 3.2 25.3 1.0 O3A B:ADP238 3.3 29.3 1.0 O2B B:ADP238 3.9 33.0 1.0 NZ B:LYS13 4.0 18.8 1.0 OD1 B:ASP191 4.0 20.7 1.0 OD2 B:ASP191 4.1 20.8 1.0 OE1 B:GLU179 4.1 22.5 1.0 NZ B:LYS177 4.2 27.8 1.0 O1A B:ADP238 4.3 30.1 1.0 NZ B:LYS123 4.3 26.3 1.0 O1B B:ADP238 4.3 28.6 1.0 O B:HOH321 4.4 40.7 1.0 O5' B:ADP238 4.4 32.0 1.0 O B:HOH252 4.4 30.5 1.0 CG B:ASP191 4.5 20.2 1.0 O B:HOH354 4.9 35.2 1.0 C5' B:ADP238 5.0 26.8 1.0

N.D.Ginder, D.J.Binkowski, H.J.Fromm, R.B.Honzatko. Nucleotide Complexes of Escherichia Coli Phosphoribosylaminoimidazole Succinocarboxamide Synthetase. J.Biol.Chem. V. 281 20680 2006.
ISSN: ISSN 0021-9258
PubMed: 16687397
DOI: 10.1074/JBC.M602109200