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Magnesium in PDB 1ajb: Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity

Enzymatic activity of Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity

All present enzymatic activity of Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity:
3.1.3.1;

Protein crystallography data

The structure of Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity, PDB code: 1ajb was solved by C.G.Dealwis, L.Chen, C.Abad-Zapatero, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.50
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 195.020, 166.930, 76.440, 90.00, 90.00, 90.00
R / Rfree (%) 16.2 / n/a

Other elements in 1ajb:

The structure of Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity also contains other interesting chemical elements:

Zinc (Zn) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity (pdb code 1ajb). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity, PDB code: 1ajb:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1ajb

Go back to Magnesium Binding Sites List in 1ajb
Magnesium binding site 1 out of 2 in the Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg452

b:26.2
occ:1.00
 OD2 A:ASP51 2.0 13.1 1.0
O A:HOH460 2.0 23.3 1.0
O A:HOH458 2.2 0.0 0.0
OE2 A:GLU322 2.4 10.8 1.0
O A:HOH459 2.5 8.7 1.0
OG1 A:THR155 2.7 9.6 1.0
CG A:ASP51 3.0 8.8 1.0
CD A:GLU322 3.3 9.1 1.0
OE1 A:GLU322 3.6 8.3 1.0
CB A:THR155 3.6 8.2 1.0
CB A:ASP51 3.7 4.2 1.0
OD1 A:ASP51 3.8 7.4 1.0
N A:THR155 4.1 6.4 1.0
O A:HOH543 4.1 0.0 0.0
OG A:SER102 4.2 3.3 1.0
O A:HOH478 4.2 9.8 1.0
O2 A:SO4457 4.3 16.3 1.0
O A:HOH527 4.3 0.0 0.0
CA A:THR155 4.5 6.7 1.0
CB A:SER102 4.6 2.0 1.0
CG A:GLU322 4.6 4.6 1.0
ZN A:ZN451 4.6 18.2 1.0
O A:ALA324 4.7 9.0 1.0
CG2 A:THR155 4.7 2.0 1.0
CA A:ALA324 4.8 6.3 1.0
CB A:ALA324 4.8 2.1 1.0
OD2 A:ASP369 5.0 5.8 1.0
CD A:PRO156 5.0 6.8 1.0

Magnesium binding site 2 out of 2 in 1ajb

Go back to Magnesium Binding Sites List in 1ajb
Magnesium binding site 2 out of 2 in the Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg952

b:19.4
occ:1.00
 O B:HOH958 2.3 10.9 1.0
O B:HOH960 2.4 18.6 1.0
OG1 B:THR155 2.4 13.2 1.0
O B:HOH959 2.5 32.1 1.0
OD2 B:ASP51 2.6 14.4 1.0
OE2 B:GLU322 2.7 11.2 1.0
O3 B:SO4957 3.3 22.2 1.0
CB B:THR155 3.5 10.7 1.0
CD B:GLU322 3.6 9.7 1.0
OE1 B:GLU322 3.7 13.2 1.0
CG B:ASP51 3.7 10.7 1.0
O B:HOH972 3.7 2.0 1.0
N B:THR155 3.9 10.6 1.0
CA B:THR155 4.4 12.0 1.0
S B:SO4957 4.4 19.1 1.0
OD1 B:ASP51 4.4 8.9 1.0
O2 B:SO4957 4.5 28.1 1.0
N B:ALA154 4.5 10.5 1.0
CB B:ASP51 4.5 10.1 1.0
CB B:SER102 4.5 6.0 1.0
CG2 B:THR155 4.6 6.7 1.0
OG B:SER102 4.8 4.7 1.0
CB B:ALA154 4.8 6.0 1.0
C B:GLY153 4.8 10.7 1.0
CB B:ALA324 4.9 2.0 1.0
C B:ALA154 4.9 9.3 1.0
CA B:ALA154 4.9 9.1 1.0
CB B:ALA149 4.9 14.3 1.0
CD B:PRO156 5.0 11.5 1.0

Reference:

C.G.Dealwis, L.Chen, C.Brennan, W.Mandecki, C.Abad-Zapatero. 3-D Structure of the D153G Mutant of Escherichia Coli Alkaline Phosphatase: An Enzyme with Weaker Magnesium Binding and Increased Catalytic Activity. Protein Eng. V. 8 865 1995.
ISSN: ISSN 0269-2139
PubMed: 8746724
DOI: 10.1093/PROTEIN/8.9.865
Page generated: Tue Aug 13 02:03:39 2024

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