Magnesium in PDB 2gcq: Fully Ligated E.Coli Adenylosuccinate Synthetase with Gtp, 2'-Deoxy- Imp and Hadacidin

All present enzymatic activity of Fully Ligated E.Coli Adenylosuccinate Synthetase with Gtp, 2'-Deoxy- Imp and Hadacidin:
6.3.4.4;

The structure of Fully Ligated E.Coli Adenylosuccinate Synthetase with Gtp, 2'-Deoxy- Imp and Hadacidin, PDB code: 2gcq was solved by R.B.Honzatko, Y.Zhou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.00
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	80.585, 80.585, 158.460, 90.00, 90.00, 120.00
R / Rfree (%)	22.4 / 25.1

The binding sites of Magnesium atom in the Fully Ligated E.Coli Adenylosuccinate Synthetase with Gtp, 2'-Deoxy- Imp and Hadacidin (pdb code 2gcq). 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 Fully Ligated E.Coli Adenylosuccinate Synthetase with Gtp, 2'-Deoxy- Imp and Hadacidin, PDB code: 2gcq:

Magnesium binding site 1 out of 1 in the Fully Ligated E.Coli Adenylosuccinate Synthetase with Gtp, 2'-Deoxy- Imp and Hadacidin


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Fully Ligated E.Coli Adenylosuccinate Synthetase with Gtp, 2'-Deoxy- Imp and Hadacidin within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg435 b:36.9 occ:1.00 O2A A:GDP432 2.0 38.5 1.0 O A:GLY40 2.1 34.3 1.0 OD1 A:ASP13 2.1 33.4 1.0 O2B A:GDP432 2.2 28.5 1.0 O16 A:DOI451 2.2 41.1 1.0 O A:HDA437 2.2 39.5 1.0 C A:HDA437 3.0 40.8 1.0 C A:GLY40 3.1 34.3 1.0 PA A:GDP432 3.2 35.7 1.0 CG A:ASP13 3.3 32.7 1.0 PB A:GDP432 3.5 31.5 1.0 P6 A:DOI451 3.5 42.9 1.0 O3A A:GDP432 3.6 33.2 1.0 N A:GLY40 3.6 34.3 1.0 CA A:GLY40 3.6 34.5 1.0 O36 A:DOI451 3.7 41.7 1.0 NA A:HDA437 3.9 42.4 1.0 CA A:ASP13 4.0 30.9 1.0 NH2 A:ARG305 4.0 44.6 1.0 CB A:ASP13 4.0 30.1 1.0 OB A:HDA437 4.1 40.9 1.0 O1A A:GDP432 4.1 36.7 1.0 ND1 A:HIS41 4.1 39.2 1.0 CB A:ALA299 4.2 43.0 1.0 N A:HIS41 4.2 34.4 1.0 OD2 A:ASP13 4.3 32.4 1.0 O1B A:GDP432 4.3 30.6 1.0 N A:ASP13 4.3 30.1 1.0 O5' A:GDP432 4.4 36.3 1.0 N1 A:DOI451 4.4 34.9 1.0 O6 A:DOI451 4.5 38.1 1.0 O26 A:DOI451 4.5 40.4 1.0 O3B A:GDP432 4.6 32.6 1.0 CA A:HIS41 4.6 36.3 1.0 C6 A:DOI451 4.7 36.1 1.0 CE1 A:HIS41 4.7 37.5 1.0 N A:ALA299 4.9 45.3 1.0 C A:ALA39 4.9 33.7 1.0

C.V.Iancu, Y.Zhou, T.Borza, H.J.Fromm, R.B.Honzatko. Cavitation As A Mechanism of Substrate Discrimination By Adenylosuccinate Synthetases Biochemistry V. 45 11703 2006.
ISSN: ISSN 0006-2960
PubMed: 16981730
DOI: 10.1021/BI0607498