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

Enzymatic activity of E. Coli Aspartate Transcarbamoylase Complexed with Dctp, Utp, and MG2+

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

Protein crystallography data

The structure of E. Coli Aspartate Transcarbamoylase Complexed with Dctp, Utp, and MG2+, PDB code: 4fyx 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) 49.22 / 2.09
Space group P 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 121.210, 121.210, 141.764, 90.00, 90.00, 120.00
R / Rfree (%) 16.5 / 21.3

Other elements in 4fyx:

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

Zinc (Zn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the E. Coli Aspartate Transcarbamoylase Complexed with Dctp, Utp, and MG2+ (pdb code 4fyx). 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 Dctp, Utp, and MG2+, PDB code: 4fyx:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 4fyx

Go back to Magnesium Binding Sites List in 4fyx
Magnesium binding site 1 out of 2 in the E. Coli Aspartate Transcarbamoylase Complexed with Dctp, 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 Dctp, Utp, and MG2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg204

b:47.1
occ:1.00
O3G B:DCP203 2.0 50.5 1.0
O2B B:DCP203 2.0 41.0 1.0
O3G B:UTP202 2.0 43.9 1.0
O B:HOH307 2.1 45.5 1.0
O1B B:UTP202 2.1 36.2 1.0
O B:HOH306 2.2 37.0 1.0
PG B:DCP203 3.1 53.3 1.0
PB B:DCP203 3.3 50.3 1.0
PG B:UTP202 3.4 51.2 1.0
PB B:UTP202 3.4 50.3 1.0
O1G B:DCP203 3.6 53.4 1.0
O3B B:DCP203 3.6 59.2 1.0
O3B B:UTP202 3.7 0.3 1.0
NE2 B:HIS20 3.8 36.6 1.0
O3A B:DCP203 4.1 41.8 1.0
O2B B:UTP202 4.2 57.0 1.0
O1A B:UTP202 4.2 43.2 1.0
O2G B:UTP202 4.2 42.8 1.0
O1B B:DCP203 4.4 57.1 1.0
CE1 B:HIS20 4.4 38.3 1.0
O2G B:DCP203 4.4 55.5 1.0
O1G B:UTP202 4.4 58.6 1.0
OD1 B:ASP19 4.5 38.6 1.0
O3A B:UTP202 4.5 41.5 1.0
PA B:UTP202 4.8 45.1 1.0
O2A B:UTP202 4.9 43.3 1.0
NZ B:LYS56 4.9 44.1 1.0
CD2 B:HIS20 5.0 40.8 1.0

Magnesium binding site 2 out of 2 in 4fyx

Go back to Magnesium Binding Sites List in 4fyx
Magnesium binding site 2 out of 2 in the E. Coli Aspartate Transcarbamoylase Complexed with Dctp, 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 Dctp, Utp, and MG2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg204

b:43.4
occ:1.00
O2B D:DCP203 2.0 39.5 1.0
O2G D:UTP202 2.0 37.6 0.9
O3G D:DCP203 2.1 36.1 1.0
O D:HOH321 2.1 36.6 1.0
O D:HOH320 2.1 38.1 1.0
O2B D:UTP202 2.1 32.2 0.9
PG D:UTP202 3.2 47.3 0.9
PB D:UTP202 3.3 44.4 0.9
PG D:DCP203 3.3 47.0 1.0
PB D:DCP203 3.4 42.5 1.0
O3B D:UTP202 3.5 44.4 0.9
O3B D:DCP203 3.7 46.4 1.0
NE2 D:HIS20 3.8 39.8 1.0
O2G D:DCP203 3.9 49.4 1.0
O2A D:UTP202 3.9 40.6 0.9
O3A D:DCP203 4.2 39.7 1.0
O1B D:UTP202 4.2 46.4 0.9
O3G D:UTP202 4.2 47.1 0.9
O1G D:UTP202 4.3 52.1 0.9
O1B D:DCP203 4.3 52.9 1.0
O3A D:UTP202 4.4 45.5 0.9
CE1 D:HIS20 4.4 45.2 1.0
O1G D:DCP203 4.5 51.1 1.0
OD2 D:ASP19 4.6 37.3 1.0
PA D:UTP202 4.6 45.2 0.9
OE2 D:GLU52 4.7 0.8 1.0
O1A D:UTP202 4.8 35.5 0.9
NZ D:LYS56 4.8 34.8 1.0
CD2 D:HIS20 4.9 36.1 1.0

Reference:

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
Page generated: Mon Dec 14 15:49:15 2020

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