Magnesium in PDB 4kh1: The R State Structure of E. Coli Atcase with Ctp,Utp, and Magnesium Bound

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

The structure of The R State Structure of E. Coli Atcase with Ctp,Utp, and Magnesium Bound, PDB code: 4kh1 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)	31.81 / 2.20
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	120.870, 120.870, 154.730, 90.00, 90.00, 120.00
R / Rfree (%)	16.3 / 19.6

The structure of The R State Structure of E. Coli Atcase with Ctp,Utp, 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 Ctp,Utp, and Magnesium Bound (pdb code 4kh1). 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 Ctp,Utp, and Magnesium Bound, PDB code: 4kh1:
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 Ctp,Utp, 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 Ctp,Utp, and Magnesium Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg204 b:94.8 occ:0.79 O2B B:CTP202 2.0 76.5 0.8 O1B B:UTP203 2.0 75.4 0.7 O B:HOH302 2.1 86.1 1.0 O2G B:UTP203 2.1 78.6 0.7 O B:HOH301 2.1 89.2 1.0 O1G B:CTP202 2.2 75.7 0.8 PG B:CTP202 3.2 81.5 0.8 PB B:CTP202 3.3 85.0 0.8 PG B:UTP203 3.3 81.1 0.7 PB B:UTP203 3.3 75.7 0.7 O2G B:CTP202 3.6 85.2 0.8 O3B B:CTP202 3.6 72.1 0.8 O3B B:UTP203 3.6 0.1 0.7 NE2 B:HIS20 3.8 78.0 1.0 O1G B:UTP203 3.9 79.3 0.7 O3A B:UTP203 4.1 81.3 0.7 O3A B:CTP202 4.2 67.0 0.8 CE1 B:HIS20 4.2 84.3 1.0 O1B B:CTP202 4.4 85.9 0.8 O2B B:UTP203 4.4 87.8 0.7 O3G B:UTP203 4.5 71.0 0.7 O3G B:CTP202 4.5 84.8 0.8 O1A B:UTP203 4.6 99.5 0.7 OD2 B:ASP19 4.6 68.2 1.0 PA B:UTP203 4.8 97.3 0.7

Magnesium binding site 2 out of 2 in the The R State Structure of E. Coli Atcase with Ctp,Utp, 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 Ctp,Utp, and Magnesium Bound within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg204 b:62.9 occ:0.58 O1B D:UTP203 1.8 0.9 0.8 O2G D:CTP202 2.0 93.8 0.8 O D:HOH302 2.0 77.2 1.0 O2B D:CTP202 2.1 81.2 0.8 O D:HOH301 2.1 79.2 1.0 O1G D:UTP203 2.4 80.2 0.8 PB D:UTP203 3.3 0.3 0.8 PG D:CTP202 3.3 95.1 0.8 PB D:CTP202 3.3 80.8 0.8 PG D:UTP203 3.6 80.6 0.8 O3B D:CTP202 3.6 76.5 0.8 O3B D:UTP203 3.7 0.4 0.8 O3A D:UTP203 4.0 0.6 0.8 O1G D:CTP202 4.1 97.0 0.8 NE2 D:HIS20 4.1 86.0 1.0 O3A D:CTP202 4.2 77.2 0.8 O2A D:UTP203 4.2 93.1 0.8 CE1 D:HIS20 4.3 87.0 1.0 O2B D:UTP203 4.3 0.1 0.8 O3G D:CTP202 4.3 95.2 0.8 O3G D:UTP203 4.3 0.7 0.8 OD2 D:ASP19 4.4 76.1 1.0 O1B D:CTP202 4.5 86.3 0.8 PA D:UTP203 4.5 96.0 0.8 O1A D:UTP203 4.6 96.6 0.8 O2G D:UTP203 4.8 82.7 0.8 NZ D:LYS56 4.8 74.0 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