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Magnesium in PDB 1ajc: 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: 1ajc 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 1ajc:

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 1ajc). 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: 1ajc:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1ajc

Go back to Magnesium Binding Sites List in 1ajc
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:14.3
occ:1.00
 OE2 A:GLU322 2.1 13.1 1.0
O A:HOH456 2.1 27.9 1.0
OD2 A:ASP51 2.1 24.4 1.0
CG A:ASP51 2.9 22.4 1.0
OG1 A:THR155 2.9 9.3 1.0
O A:HOH455 3.0 9.6 1.0
CD A:GLU322 3.3 13.5 1.0
OD1 A:ASP51 3.3 24.4 1.0
CB A:THR155 3.5 12.9 1.0
N A:THR155 3.7 8.9 1.0
OE1 A:GLU322 3.7 11.5 1.0
CB A:ASP51 4.1 10.0 1.0
CA A:THR155 4.2 7.5 1.0
OG A:SER102 4.3 21.9 1.0
CB A:SER102 4.4 19.0 1.0
CG A:GLU322 4.5 13.2 1.0
N A:ALA154 4.6 11.8 1.0
C A:ALA154 4.7 10.5 1.0
CG2 A:THR155 4.7 4.8 1.0
CB A:ALA154 4.8 11.6 1.0
ZN A:ZN451 4.8 52.3 1.0
CA A:ALA154 4.9 12.4 1.0
CD A:PRO156 4.9 13.1 1.0

Magnesium binding site 2 out of 2 in 1ajc

Go back to Magnesium Binding Sites List in 1ajc
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:24.5
occ:1.00
 OD2 B:ASP51 2.0 24.3 1.0
OE2 B:GLU322 2.3 17.5 1.0
O B:HOH956 2.4 18.0 1.0
OG1 B:THR155 2.6 13.9 1.0
CG B:ASP51 2.9 22.2 1.0
CD B:GLU322 3.1 18.3 1.0
CB B:THR155 3.1 16.2 1.0
OD1 B:ASP51 3.1 23.1 1.0
OE1 B:GLU322 3.1 14.3 1.0
N B:THR155 3.7 17.3 1.0
CA B:THR155 4.0 15.6 1.0
CB B:ASP51 4.2 13.5 1.0
CG2 B:THR155 4.3 13.6 1.0
CG B:GLU322 4.5 18.0 1.0
CD B:PRO156 4.6 16.2 1.0
OG B:SER102 4.8 22.4 1.0
ZN B:ZN951 4.9 47.9 1.0
C B:ALA154 4.9 14.9 1.0
OD2 B:ASP369 4.9 16.4 1.0
CB B:SER102 4.9 23.1 1.0

Reference:

C.G.Dealwis, C.Brennan, K.Christianson, W.Mandecki, C.Abad-Zapatero. Crystallographic Analysis of Reversible Metal Binding Observed in A Mutant (ASP153-->Gly) of Escherichia Coli Alkaline Phosphatase. Biochemistry V. 34 13967 1995.
ISSN: ISSN 0006-2960
PubMed: 7577993
DOI: 10.1021/BI00043A001
Page generated: Tue Aug 13 02:04:39 2024

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