Magnesium in PDB 4kh0: The R State Structure of E. Coli Atcase with Atp and Magnesium Bound

All present enzymatic activity of The R State Structure of E. Coli Atcase with Atp and Magnesium Bound:
2.1.3.2;

The structure of The R State Structure of E. Coli Atcase with Atp and Magnesium Bound, PDB code: 4kh0 was solved by G.M.Cockrell, Y.Zheng, W.Guo, A.W.Peterson, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.69 / 2.25
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	121.133, 121.133, 155.107, 90.00, 90.00, 120.00
R / Rfree (%)	16.8 / 20.8

The structure of The R State Structure of E. Coli Atcase with Atp and Magnesium Bound also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Magnesium atom in the The R State Structure of E. Coli Atcase with Atp and Magnesium Bound (pdb code 4kh0). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The R State Structure of E. Coli Atcase with Atp and Magnesium Bound, PDB code: 4kh0:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the The R State Structure of E. Coli Atcase with Atp and Magnesium Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The R State Structure of E. Coli Atcase with Atp and Magnesium Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg204 b:84.3 occ:1.00 O3G B:ATP203 1.7 97.2 1.0 O2B B:ATP202 1.9 64.0 1.0 O1B B:ATP203 2.0 89.4 1.0 O B:HOH302 2.1 68.0 1.0 O1G B:ATP202 2.2 66.8 1.0 PB B:ATP202 3.1 78.8 1.0 PG B:ATP203 3.1 98.9 1.0 O3B B:ATP202 3.3 75.9 1.0 PG B:ATP202 3.3 77.6 1.0 PB B:ATP203 3.3 86.1 1.0 O B:HOH301 3.4 64.7 1.0 O3B B:ATP203 3.6 0.9 1.0 NZ D:LYS6 3.6 0.9 1.0 NE2 B:HIS20 3.8 61.1 1.0 O1G B:ATP203 4.0 98.1 1.0 O3A B:ATP202 4.1 52.8 1.0 O2G B:ATP202 4.1 87.7 1.0 CE1 B:HIS20 4.2 64.3 1.0 CE D:LYS6 4.2 1.0 1.0 O2G B:ATP203 4.2 0.4 1.0 O1B B:ATP202 4.2 83.9 1.0 O2B B:ATP203 4.3 92.1 1.0 O3G B:ATP202 4.4 84.9 1.0 O3A B:ATP203 4.5 0.1 1.0 O2A B:ATP203 4.5 0.6 1.0 OD2 B:ASP19 4.6 50.9 1.0 PA B:ATP203 4.8 0.1 1.0 O1A B:ATP203 4.8 0.5 1.0 NZ B:LYS56 5.0 53.5 1.0 CD2 B:HIS20 5.0 59.9 1.0

Magnesium binding site 2 out of 2 in the The R State Structure of E. Coli Atcase with Atp and Magnesium Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The R State Structure of E. Coli Atcase with Atp and Magnesium Bound within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg204 b:67.8 occ:1.00 O2B D:ATP202 1.9 68.6 1.0 O2G D:ATP202 2.0 73.1 1.0 O1G D:ATP203 2.0 66.4 1.0 O2B D:ATP203 2.1 83.6 1.0 O D:HOH301 2.1 71.6 1.0 O D:HOH302 2.1 50.3 1.0 PB D:ATP202 3.1 68.0 1.0 PG D:ATP202 3.2 71.5 1.0 PG D:ATP203 3.4 73.6 1.0 PB D:ATP203 3.4 82.2 1.0 O3B D:ATP202 3.4 55.6 1.0 O3B D:ATP203 3.8 96.0 1.0 O1G D:ATP202 3.9 71.8 1.0 O3A D:ATP203 3.9 0.9 1.0 NE2 D:HIS20 4.0 50.6 1.0 O2G D:ATP203 4.0 77.0 1.0 O1B D:ATP202 4.1 74.1 1.0 O3A D:ATP202 4.2 49.0 1.0 O3G D:ATP202 4.4 69.9 1.0 O3G D:ATP203 4.5 77.7 1.0 CE1 D:HIS20 4.5 57.5 1.0 O1B D:ATP203 4.7 81.9 1.0 NZ B:LYS6 4.7 92.4 1.0 OD2 D:ASP19 4.8 60.6 1.0

G.M.Cockrell, Y.Zheng, W.Guo, A.W.Peterson, J.K.Truong, E.R.Kantrowitz. New Paradigm For Allosteric Regulation of Escherichia Coli Aspartate Transcarbamoylase. Biochemistry V. 52 8036 2013.
ISSN: ISSN 0006-2960
PubMed: 24138583
DOI: 10.1021/BI401205N