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Magnesium in PDB 1cg3: Structure of the Mutant (R143L) of Adenylosuccinate Synthetase From E. Coli Complexed with Hadacidin, Gdp, 6-Phosphoryl-Imp, and MG2+

Enzymatic activity of Structure of the Mutant (R143L) of Adenylosuccinate Synthetase From E. Coli Complexed with Hadacidin, Gdp, 6-Phosphoryl-Imp, and MG2+

All present enzymatic activity of Structure of the Mutant (R143L) of Adenylosuccinate Synthetase From E. Coli Complexed with Hadacidin, Gdp, 6-Phosphoryl-Imp, and MG2+:
6.3.4.4;

Protein crystallography data

The structure of Structure of the Mutant (R143L) of Adenylosuccinate Synthetase From E. Coli Complexed with Hadacidin, Gdp, 6-Phosphoryl-Imp, and MG2+, PDB code: 1cg3 was solved by J.Y.Choe, B.W.Poland, H.Fromm, R.Honzatko, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 5.00 / 2.50
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 80.940, 80.940, 158.180, 90.00, 90.00, 120.00
R / Rfree (%) 16.2 / 23.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the Mutant (R143L) of Adenylosuccinate Synthetase From E. Coli Complexed with Hadacidin, Gdp, 6-Phosphoryl-Imp, and MG2+ (pdb code 1cg3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Structure of the Mutant (R143L) of Adenylosuccinate Synthetase From E. Coli Complexed with Hadacidin, Gdp, 6-Phosphoryl-Imp, and MG2+, PDB code: 1cg3:

Magnesium binding site 1 out of 1 in 1cg3

Go back to Magnesium Binding Sites List in 1cg3
Magnesium binding site 1 out of 1 in the Structure of the Mutant (R143L) of Adenylosuccinate Synthetase From E. Coli Complexed with Hadacidin, Gdp, 6-Phosphoryl-Imp, and MG2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Mutant (R143L) of Adenylosuccinate Synthetase From E. Coli Complexed with Hadacidin, Gdp, 6-Phosphoryl-Imp, and MG2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg435

b:15.0
occ:1.00
 O A:GLY40 2.0 16.8 1.0
O2B A:GDP432 2.1 10.3 1.0
O A:HDA437 2.1 21.0 1.0
O1 A:IMO440 2.1 14.8 1.0
OD1 A:ASP13 2.2 16.6 1.0
O2A A:GDP432 2.2 21.2 1.0
C A:HDA437 3.1 19.4 1.0
C A:GLY40 3.2 16.1 1.0
PA A:GDP432 3.2 19.9 1.0
CG A:ASP13 3.3 16.9 1.0
PB A:GDP432 3.4 12.4 1.0
P A:IMO440 3.5 16.4 1.0
O3A A:GDP432 3.5 16.1 1.0
O2 A:IMO440 3.7 11.2 1.0
NH2 A:ARG305 3.7 15.8 1.0
N A:GLY40 3.8 15.1 1.0
CA A:GLY40 3.8 13.1 1.0
CA A:ASP13 3.9 10.3 1.0
NA A:HDA437 4.0 19.2 1.0
O1A A:GDP432 4.0 21.7 1.0
CB A:ASP13 4.0 7.7 1.0
OB A:HDA437 4.2 19.9 1.0
CB A:ALA299 4.2 16.9 1.0
OD2 A:ASP13 4.3 14.5 1.0
N A:HIS41 4.3 13.5 1.0
N A:ASP13 4.3 13.4 1.0
O1B A:GDP432 4.3 15.6 1.0
O3 A:IMO440 4.4 7.3 1.0
O3B A:GDP432 4.4 9.3 1.0
CD2 A:HIS41 4.5 11.6 1.0
O5' A:GDP432 4.5 16.0 1.0
O6 A:IMO440 4.5 15.4 1.0
N1 A:IMO440 4.5 12.1 1.0
CA A:HIS41 4.6 15.6 1.0
CZ A:ARG305 4.8 18.4 1.0
C6 A:IMO440 4.9 10.0 1.0

Reference:

J.Y.Choe, B.W.Poland, H.J.Fromm, R.B.Honzatko. Mechanistic Implications From Crystalline Complexes of Wild-Type and Mutant Adenylosuccinate Synthetases From Escherichia Coli. Biochemistry V. 38 6953 1999.
ISSN: ISSN 0006-2960
PubMed: 10346917
DOI: 10.1021/BI990159S
Page generated: Tue Aug 13 02:28:40 2024

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