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

Enzymatic activity of The R State Structure of E. Coli Atcase with Utp and Magnesium Bound

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

Protein crystallography data

The structure of The R State Structure of E. Coli Atcase with Utp and Magnesium Bound, PDB code: 4kgz 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) 49.78 / 2.40
Space group P 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 121.378, 121.378, 155.135, 90.00, 90.00, 120.00
R / Rfree (%) 16.5 / 20.3

Other elements in 4kgz:

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

Zinc (Zn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The R State Structure of E. Coli Atcase with Utp and Magnesium Bound (pdb code 4kgz). 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 Utp and Magnesium Bound, PDB code: 4kgz:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 4kgz

Go back to Magnesium Binding Sites List in 4kgz
Magnesium binding site 1 out of 2 in the The R State Structure of E. Coli Atcase with 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 Utp and Magnesium Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg204

b:0.5
occ:0.64
O1G B:UTP202 1.6 95.5 0.7
O B:HOH301 2.1 81.9 1.0
O B:HOH302 2.1 0.4 1.0
O2B B:UTP202 2.1 83.1 0.7
O1B B:UTP203 2.1 90.5 0.8
O2G B:UTP203 2.2 89.7 0.8
PG B:UTP202 3.0 94.2 0.7
PB B:UTP202 3.3 81.7 0.7
PB B:UTP203 3.4 90.6 0.8
PG B:UTP203 3.5 89.8 0.8
O3B B:UTP202 3.5 0.6 0.7
O3B B:UTP203 3.7 0.0 0.8
O1A B:UTP203 3.7 0.4 0.8
O3A B:UTP202 3.8 79.1 0.7
NE2 B:HIS20 3.8 71.3 1.0
O2G B:UTP202 3.9 92.5 0.7
O3G B:UTP202 4.0 0.8 0.7
CE1 B:HIS20 4.1 79.0 1.0
OD2 B:ASP19 4.1 69.0 1.0
O3A B:UTP203 4.4 93.6 0.8
PA B:UTP203 4.4 0.8 0.8
O3G B:UTP203 4.4 0.8 0.8
O2B B:UTP203 4.4 96.1 0.8
O2A B:UTP203 4.4 0.4 0.8
O1G B:UTP203 4.5 87.5 0.8
O1B B:UTP202 4.6 82.6 0.7
NZ B:LYS56 4.6 64.5 1.0
CG B:ASP19 5.0 69.6 1.0

Magnesium binding site 2 out of 2 in 4kgz

Go back to Magnesium Binding Sites List in 4kgz
Magnesium binding site 2 out of 2 in the The R State Structure of E. Coli Atcase with 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 Utp and Magnesium Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg204

b:0.5
occ:1.00
O2G D:UTP202 1.8 0.8 1.0
O D:HOH302 2.1 75.8 1.0
O D:HOH301 2.1 58.0 1.0
O1G D:UTP203 2.2 0.7 1.0
O1B D:UTP203 2.2 0.7 1.0
O2B D:UTP202 2.2 1.0 1.0
PG D:UTP202 3.1 0.8 1.0
PB D:UTP202 3.4 0.5 1.0
O3B D:UTP202 3.4 0.4 1.0
PG D:UTP203 3.5 0.6 1.0
PB D:UTP203 3.6 0.4 1.0
O1A D:UTP203 3.8 0.6 1.0
O3B D:UTP203 3.8 0.0 1.0
O3G D:UTP202 4.0 81.6 1.0
CE1 D:HIS20 4.0 82.5 1.0
NE2 D:HIS20 4.0 83.0 1.0
OD2 D:ASP19 4.1 68.5 1.0
O1G D:UTP202 4.1 0.8 1.0
O3A D:UTP202 4.3 0.3 1.0
O3G D:UTP203 4.4 77.1 1.0
O2B D:UTP203 4.5 0.6 1.0
O1B D:UTP202 4.5 0.1 1.0
PA D:UTP203 4.5 0.9 1.0
O3A D:UTP203 4.5 0.1 1.0
O2A D:UTP203 4.5 0.7 1.0
O2G D:UTP203 4.5 0.2 1.0
NZ D:LYS56 4.6 62.3 1.0
O D:HOH318 4.9 67.8 1.0
O2A D:UTP202 4.9 0.1 1.0

Reference:

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
Page generated: Mon Dec 14 19:02:50 2020

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