Magnesium in PDB 4fyy: E. Coli Aspartate Transcarbamoylase Complexed with Ctp, Utp, and MG2+

All present enzymatic activity of E. Coli Aspartate Transcarbamoylase Complexed with Ctp, Utp, and MG2+:
2.1.3.2;

The structure of E. Coli Aspartate Transcarbamoylase Complexed with Ctp, Utp, and MG2+, PDB code: 4fyy was solved by G.M.Cockrell, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.18 / 1.94
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	121.133, 121.133, 141.438, 90.00, 90.00, 120.00
R / Rfree (%)	19.3 / 23.7

The structure of E. Coli Aspartate Transcarbamoylase Complexed with Ctp, Utp, and MG2+ also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Magnesium atom in the E. Coli Aspartate Transcarbamoylase Complexed with Ctp, Utp, and MG2+ (pdb code 4fyy). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the E. Coli Aspartate Transcarbamoylase Complexed with Ctp, Utp, and MG2+, PDB code: 4fyy:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the E. Coli Aspartate Transcarbamoylase Complexed with Ctp, Utp, and MG2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of E. Coli Aspartate Transcarbamoylase Complexed with Ctp, Utp, and MG2+ within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg204 b:45.5 occ:1.00 O1G B:UTP202 1.8 44.8 1.0 O2G B:CTP203 2.0 45.1 1.0 O B:HOH301 2.1 46.3 1.0 O B:HOH302 2.1 49.5 1.0 O1B B:UTP202 2.2 44.2 1.0 O1B B:CTP203 2.2 45.4 1.0 PG B:UTP202 3.2 52.9 1.0 PG B:CTP203 3.2 55.8 1.0 PB B:UTP202 3.4 53.6 1.0 PB B:CTP203 3.5 52.9 1.0 O3B B:UTP202 3.7 94.8 1.0 O3G B:CTP203 3.7 62.6 1.0 O B:HOH358 3.8 70.4 1.0 O3B B:CTP203 3.8 77.2 1.0 NE2 B:HIS20 3.8 53.6 1.0 O2G B:UTP202 4.1 41.2 1.0 O2B B:UTP202 4.2 54.1 1.0 O3G B:UTP202 4.2 46.3 1.0 CE1 B:HIS20 4.3 52.3 1.0 O1A B:UTP202 4.3 40.9 1.0 O1G B:CTP203 4.4 51.9 1.0 O3A B:CTP203 4.4 39.6 1.0 O2B B:CTP203 4.5 60.1 1.0 OD1 B:ASP19 4.5 42.7 1.0 O3A B:UTP202 4.6 49.5 1.0 OE1 B:GLU52 4.9 0.4 1.0 PA B:UTP202 4.9 47.8 1.0 NZ B:LYS56 4.9 38.8 1.0

Magnesium binding site 2 out of 2 in the E. Coli Aspartate Transcarbamoylase Complexed with Ctp, Utp, and MG2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of E. Coli Aspartate Transcarbamoylase Complexed with Ctp, Utp, and MG2+ within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg204 b:44.4 occ:1.00 O1G D:UTP202 1.8 40.8 1.0 O1B D:CTP203 1.9 41.9 1.0 O2B D:UTP202 2.0 47.9 1.0 O D:HOH385 2.1 44.0 1.0 O3G D:CTP203 2.1 45.0 1.0 O D:HOH317 2.1 56.2 1.0 PG D:UTP202 3.0 54.9 1.0 PB D:UTP202 3.1 49.8 1.0 PG D:CTP203 3.3 60.1 1.0 PB D:CTP203 3.3 44.9 1.0 O3B D:UTP202 3.3 72.5 1.0 O3B D:CTP203 3.7 61.4 1.0 O1G D:CTP203 3.8 59.9 1.0 O3G D:UTP202 3.9 55.2 1.0 O1B D:UTP202 3.9 53.1 1.0 NE2 D:HIS20 4.0 50.0 1.0 O2G D:UTP202 4.1 70.0 1.0 O2A D:UTP202 4.2 57.2 1.0 O2B D:CTP203 4.2 52.2 1.0 O3A D:CTP203 4.3 40.6 1.0 O3A D:UTP202 4.3 53.2 1.0 O2G D:CTP203 4.5 64.2 1.0 CE1 D:HIS20 4.7 51.3 1.0 PA D:UTP202 4.7 52.7 1.0 OD2 D:ASP19 4.7 39.2 1.0 O1A D:UTP202 5.0 41.1 1.0

G.M.Cockrell, E.R.Kantrowitz. Metal Ion Involvement in the Allosteric Mechanism of Escherichia Coli Aspartate Transcarbamoylase. Biochemistry V. 51 7128 2012.
ISSN: ISSN 0006-2960
PubMed: 22906065
DOI: 10.1021/BI300920M