Magnesium in PDB 1lny: Crystal Structure of the Recombinant Mouse-Muscle Adenylosuccinate Synthetase Complexed with 6-Phosphoryl-Imp, Gdp and Mg

All present enzymatic activity of Crystal Structure of the Recombinant Mouse-Muscle Adenylosuccinate Synthetase Complexed with 6-Phosphoryl-Imp, Gdp and Mg:
6.3.4.4;

The structure of Crystal Structure of the Recombinant Mouse-Muscle Adenylosuccinate Synthetase Complexed with 6-Phosphoryl-Imp, Gdp and Mg, PDB code: 1lny was solved by C.V.Iancu, T.Borza, H.J.Fromm, R.B.Honzatko, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	5.00 / 2.20
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	128.500, 70.120, 105.130, 90.00, 90.46, 90.00
R / Rfree (%)	20.7 / 25.9

The binding sites of Magnesium atom in the Crystal Structure of the Recombinant Mouse-Muscle Adenylosuccinate Synthetase Complexed with 6-Phosphoryl-Imp, Gdp and Mg (pdb code 1lny). 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 the Recombinant Mouse-Muscle Adenylosuccinate Synthetase Complexed with 6-Phosphoryl-Imp, Gdp and Mg, PDB code: 1lny:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of the Recombinant Mouse-Muscle Adenylosuccinate Synthetase Complexed with 6-Phosphoryl-Imp, Gdp and Mg


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 the Recombinant Mouse-Muscle Adenylosuccinate Synthetase Complexed with 6-Phosphoryl-Imp, Gdp and Mg within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1453 b:35.8 occ:1.00 O2A A:GDP1452 1.9 36.3 1.0 O2B A:GDP1452 2.0 35.1 1.0 O A:GLY70 2.1 36.5 1.0 O1 A:IMO1451 2.1 45.1 1.0 O A:HOH817 2.1 29.0 1.0 OD1 A:ASP43 2.1 33.9 1.0 C A:GLY70 3.2 37.3 1.0 PA A:GDP1452 3.2 35.9 1.0 CG A:ASP43 3.2 36.3 1.0 P A:IMO1451 3.3 50.2 1.0 PB A:GDP1452 3.3 36.2 1.0 O3A A:GDP1452 3.5 33.1 1.0 O3 A:IMO1451 3.5 45.1 1.0 CA A:ASP43 3.8 33.0 1.0 N A:GLY70 3.8 37.2 1.0 CA A:GLY70 3.8 36.5 1.0 CB A:ASP43 3.9 34.3 1.0 CD2 A:HIS71 4.1 40.1 1.0 N A:ASP43 4.1 30.7 1.0 O1A A:GDP1452 4.2 35.8 1.0 N1 A:IMO1451 4.2 44.3 1.0 O2 A:IMO1451 4.2 46.5 1.0 O1B A:GDP1452 4.2 34.9 1.0 OD2 A:ASP43 4.2 39.0 1.0 O5' A:GDP1452 4.3 37.2 1.0 N A:HIS71 4.3 36.7 1.0 O3B A:GDP1452 4.4 33.2 1.0 O6 A:IMO1451 4.4 47.0 1.0 CA A:HIS71 4.6 37.5 1.0 C6 A:IMO1451 4.7 45.2 1.0 NH2 A:ARG337 4.8 50.3 1.0 NE2 A:HIS71 4.8 41.4 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of the Recombinant Mouse-Muscle Adenylosuccinate Synthetase Complexed with 6-Phosphoryl-Imp, Gdp and Mg


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 the Recombinant Mouse-Muscle Adenylosuccinate Synthetase Complexed with 6-Phosphoryl-Imp, Gdp and Mg within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1456 b:34.0 occ:1.00 O2A B:GDP1454 1.9 27.3 1.0 O1 B:IMO1455 2.0 42.4 1.0 O B:GLY70 2.0 31.9 1.0 OD1 B:ASP43 2.1 31.5 1.0 O2B B:GDP1454 2.1 32.6 1.0 O B:HOH696 2.3 27.4 1.0 C B:GLY70 3.1 33.5 1.0 CG B:ASP43 3.2 30.9 1.0 PA B:GDP1454 3.3 30.8 1.0 P B:IMO1455 3.4 46.5 1.0 PB B:GDP1454 3.4 29.0 1.0 O3A B:GDP1454 3.6 29.9 1.0 N B:GLY70 3.7 34.6 1.0 CA B:GLY70 3.7 33.5 1.0 CA B:ASP43 3.8 29.2 1.0 CB B:ASP43 3.8 29.6 1.0 O3 B:IMO1455 3.8 43.3 1.0 CD2 B:HIS71 4.0 32.9 1.0 N B:ASP43 4.1 28.8 1.0 O1B B:GDP1454 4.2 28.5 1.0 OD2 B:ASP43 4.2 33.3 1.0 N B:HIS71 4.2 34.0 1.0 O1A B:GDP1454 4.3 30.2 1.0 O2 B:IMO1455 4.3 45.8 1.0 O5' B:GDP1454 4.3 31.6 1.0 O6 B:IMO1455 4.4 44.1 1.0 N1 B:IMO1455 4.4 40.9 1.0 O B:HOH774 4.4 41.9 1.0 O3B B:GDP1454 4.5 30.4 1.0 CA B:HIS71 4.6 33.5 1.0 C6 B:IMO1455 4.7 42.0 1.0 NE2 B:HIS71 4.8 32.5 1.0 C B:ALA69 4.9 36.0 1.0

C.V.Iancu, T.Borza, H.J.Fromm, R.B.Honzatko. Imp, Gtp, and 6-Phosphoryl-Imp Complexes of Recombinant Mouse Muscle Adenylosuccinate Synthetase. J.Biol.Chem. V. 277 26779 2002.
ISSN: ISSN 0021-9258
PubMed: 12004071
DOI: 10.1074/JBC.M203730200