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Magnesium in PDB 1ed9: Structure of E. Coli Alkaline Phosphatase Without the Inorganic Phosphate at 1.75A Resolution

Enzymatic activity of Structure of E. Coli Alkaline Phosphatase Without the Inorganic Phosphate at 1.75A Resolution

All present enzymatic activity of Structure of E. Coli Alkaline Phosphatase Without the Inorganic Phosphate at 1.75A Resolution:
3.1.3.1;

Protein crystallography data

The structure of Structure of E. Coli Alkaline Phosphatase Without the Inorganic Phosphate at 1.75A Resolution, PDB code: 1ed9 was solved by B.Stec, K.M.Holtz, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 1.75
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 194.470, 167.300, 76.551, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 22.4

Other elements in 1ed9:

The structure of Structure of E. Coli Alkaline Phosphatase Without the Inorganic Phosphate at 1.75A Resolution also contains other interesting chemical elements:

Zinc (Zn) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of E. Coli Alkaline Phosphatase Without the Inorganic Phosphate at 1.75A Resolution (pdb code 1ed9). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of E. Coli Alkaline Phosphatase Without the Inorganic Phosphate at 1.75A Resolution, PDB code: 1ed9:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1ed9

Go back to Magnesium Binding Sites List in 1ed9
Magnesium binding site 1 out of 2 in the Structure of E. Coli Alkaline Phosphatase Without the Inorganic Phosphate at 1.75A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of E. Coli Alkaline Phosphatase Without the Inorganic Phosphate at 1.75A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg462

b:16.8
occ:1.00
OE2 A:GLU322 1.9 16.8 1.0
O A:HOH454 2.0 17.2 1.0
O A:HOH453 2.1 18.9 1.0
OD2 A:ASP51 2.1 19.2 1.0
O A:HOH455 2.1 13.3 1.0
OG1 A:THR155 2.3 11.3 1.0
CD A:GLU322 3.0 16.6 1.0
CG A:ASP51 3.1 19.3 1.0
CB A:THR155 3.2 15.4 1.0
OE1 A:GLU322 3.5 17.6 1.0
CB A:ASP51 3.7 18.4 1.0
OD2 A:ASP153 3.9 17.8 1.0
OD1 A:ASP51 4.1 14.1 1.0
N A:THR155 4.1 16.9 1.0
CG2 A:THR155 4.2 17.5 1.0
CG A:GLU322 4.2 17.0 1.0
O A:HOH1045 4.2 19.9 1.0
CA A:THR155 4.3 12.4 1.0
O A:HOH1544 4.3 40.8 1.0
CB A:ALA324 4.3 17.8 1.0
O A:HOH499 4.3 17.3 1.0
OG A:SER102 4.6 15.1 1.0
O A:ALA324 4.6 28.6 1.0
CA A:ALA324 4.6 18.4 1.0
ZN A:ZN451 4.6 18.3 1.0
CB A:SER102 4.7 14.1 1.0
CG A:ASP153 4.8 21.7 1.0
OD1 A:ASP369 4.9 17.2 1.0
CA A:ASP51 4.9 15.6 1.0

Magnesium binding site 2 out of 2 in 1ed9

Go back to Magnesium Binding Sites List in 1ed9
Magnesium binding site 2 out of 2 in the Structure of E. Coli Alkaline Phosphatase Without the Inorganic Phosphate at 1.75A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of E. Coli Alkaline Phosphatase Without the Inorganic Phosphate at 1.75A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg962

b:21.0
occ:1.00
OE1 B:GLU822 1.9 15.1 1.0
OD2 B:ASP551 2.0 24.4 1.0
O B:HOH954 2.0 24.4 1.0
O B:HOH953 2.1 23.5 1.0
O B:HOH955 2.1 23.4 1.0
OG1 B:THR655 2.3 19.7 1.0
CG B:ASP551 3.0 20.4 1.0
CD B:GLU822 3.0 15.5 1.0
CB B:THR655 3.1 19.5 1.0
OE2 B:GLU822 3.4 18.9 1.0
CB B:ASP551 3.7 20.4 1.0
OD2 B:ASP653 3.9 30.4 1.0
OD1 B:ASP551 4.0 13.3 1.0
N B:THR655 4.0 20.4 1.0
O B:HOH999 4.1 16.7 1.0
CG2 B:THR655 4.1 15.9 1.0
CA B:THR655 4.2 19.0 1.0
O B:HOH1095 4.3 25.5 1.0
CG B:GLU822 4.3 17.1 1.0
CB B:ALA824 4.4 15.8 1.0
O B:HOH1546 4.4 39.2 1.0
OG B:SER602 4.5 19.6 1.0
ZN B:ZN951 4.6 23.0 1.0
CB B:SER602 4.6 16.8 1.0
CA B:ALA824 4.7 15.4 1.0
CG B:ASP653 4.7 28.0 1.0
O B:ALA824 4.8 24.3 1.0
OD1 B:ASP869 4.9 22.1 1.0
CA B:ASP551 5.0 18.3 1.0

Reference:

B.Stec, K.M.Holtz, E.R.Kantrowitz. A Revised Mechanism For the Alkaline Phosphatase Reaction Involving Three Metal Ions. J.Mol.Biol. V. 299 1303 2000.
ISSN: ISSN 0022-2836
PubMed: 10873454
DOI: 10.1006/JMBI.2000.3799
Page generated: Tue Aug 13 02:55:57 2024

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