Magnesium in PDB 1kh5: E. Coli Alkaline Phosphatase Mutant (D330N) Mimic of the Transition States with Aluminium Fluoride

All present enzymatic activity of E. Coli Alkaline Phosphatase Mutant (D330N) Mimic of the Transition States with Aluminium Fluoride:
3.1.3.1;

The structure of E. Coli Alkaline Phosphatase Mutant (D330N) Mimic of the Transition States with Aluminium Fluoride, PDB code: 1kh5 was solved by M.H.Le Du, C.Lamoure, B.H.Muller, O.V.Bulgakov, E.Lajeunesse, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.00
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	163.620, 163.620, 138.880, 90.00, 90.00, 120.00
R / Rfree (%)	19.4 / 22.8

The structure of E. Coli Alkaline Phosphatase Mutant (D330N) Mimic of the Transition States with Aluminium Fluoride also contains other interesting chemical elements:

Fluorine	(F)	6 atoms
Aluminium	(Al)	2 atoms
Zinc	(Zn)	4 atoms

The binding sites of Magnesium atom in the E. Coli Alkaline Phosphatase Mutant (D330N) Mimic of the Transition States with Aluminium Fluoride (pdb code 1kh5). 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 Alkaline Phosphatase Mutant (D330N) Mimic of the Transition States with Aluminium Fluoride, PDB code: 1kh5:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the E. Coli Alkaline Phosphatase Mutant (D330N) Mimic of the Transition States with Aluminium Fluoride


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of E. Coli Alkaline Phosphatase Mutant (D330N) Mimic of the Transition States with Aluminium Fluoride within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg452 b:12.5 occ:1.00 OE1 A:GLU322 2.1 18.1 1.0 OG1 A:THR155 2.2 17.9 1.0 O A:HOH1077 2.2 20.3 1.0 OD2 A:ASP51 2.2 24.2 1.0 O A:HOH1002 2.2 20.8 1.0 O A:HOH1004 2.2 20.9 1.0 CD A:GLU322 3.1 20.0 1.0 CB A:THR155 3.2 18.2 1.0 CG A:ASP51 3.2 21.9 1.0 OE2 A:GLU322 3.4 20.8 1.0 CB A:ASP51 3.8 19.3 1.0 OD1 A:ASP153 3.8 24.8 1.0 N A:THR155 4.0 19.0 1.0 OD1 A:ASP51 4.1 23.5 1.0 CG2 A:THR155 4.2 14.5 1.0 O A:HOH1003 4.2 15.7 1.0 CA A:THR155 4.2 15.9 1.0 CG A:GLU322 4.4 15.0 1.0 CB A:ALA324 4.4 16.4 1.0 CG A:ASP153 4.6 24.3 1.0 CB A:SER102 4.6 18.8 1.0 CA A:ALA324 4.6 18.4 1.0 O A:HOH1198 4.6 44.4 1.0 O A:ALA324 4.7 19.6 1.0 OG A:SER102 4.7 30.4 1.0 ZN A:ZN451 4.8 25.3 1.0 F2 A:AF3453 4.8 37.8 1.0 CD A:PRO156 4.8 10.4 1.0

Magnesium binding site 2 out of 2 in the E. Coli Alkaline Phosphatase Mutant (D330N) Mimic of the Transition States with Aluminium Fluoride


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of E. Coli Alkaline Phosphatase Mutant (D330N) Mimic of the Transition States with Aluminium Fluoride within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg952 b:6.1 occ:1.00 OD2 B:ASP551 2.1 16.7 1.0 OE1 B:GLU822 2.1 16.9 1.0 OG1 B:THR655 2.2 16.2 1.0 O B:HOH1009 2.2 13.3 0.9 O B:HOH1008 2.3 16.5 0.6 O B:HOH1007 2.4 21.6 1.0 CG B:ASP551 3.1 18.6 1.0 CD B:GLU822 3.2 20.5 1.0 CB B:THR655 3.3 15.8 1.0 OE2 B:GLU822 3.6 18.5 1.0 CB B:ASP551 3.7 15.8 1.0 OD2 B:ASP653 3.9 24.8 1.0 OD1 B:ASP551 4.0 21.2 1.0 N B:THR655 4.1 19.0 1.0 O B:HOH1076 4.1 12.8 1.0 CG2 B:THR655 4.2 14.5 1.0 CA B:THR655 4.3 15.6 1.0 CB B:ALA824 4.4 16.9 1.0 O B:HOH1199 4.4 48.0 1.0 CG B:GLU822 4.5 18.5 1.0 CB B:SER602 4.5 15.3 1.0 F2 B:AF3953 4.6 32.0 1.0 ZN B:ZN951 4.6 25.5 1.0 CA B:ALA824 4.7 15.7 1.0 CG B:ASP653 4.7 24.4 1.0 O B:ALA824 4.7 19.7 1.0 OD1 B:ASP869 4.8 17.8 1.0 OG B:SER602 4.8 28.4 1.0

M.H.Le Du, C.Lamoure, B.H.Muller, O.V.Bulgakov, E.Lajeunesse, A.Menez, J.C.Boulain. Artificial Evolution of An Enzyme Active Site: Structural Studies of Three Highly Active Mutants of Escherichia Coli Alkaline Phosphatase. J.Mol.Biol. V. 316 941 2002.
ISSN: ISSN 0022-2836
PubMed: 11884134
DOI: 10.1006/JMBI.2001.5384