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Magnesium in PDB 1ali: Alkaline Phosphatase Mutant (H412N)

Enzymatic activity of Alkaline Phosphatase Mutant (H412N)

All present enzymatic activity of Alkaline Phosphatase Mutant (H412N):
3.1.3.1;

Protein crystallography data

The structure of Alkaline Phosphatase Mutant (H412N), PDB code: 1ali was solved by L.Ma, T.T.Tibbitts, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.20
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 194.860, 167.430, 76.530, 90.00, 90.00, 90.00
R / Rfree (%) 17.4 / n/a

Other elements in 1ali:

The structure of Alkaline Phosphatase Mutant (H412N) also contains other interesting chemical elements:

Zinc (Zn) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Alkaline Phosphatase Mutant (H412N) (pdb code 1ali). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Alkaline Phosphatase Mutant (H412N), PDB code: 1ali:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1ali

Go back to Magnesium Binding Sites List in 1ali
Magnesium binding site 1 out of 2 in the Alkaline Phosphatase Mutant (H412N)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Alkaline Phosphatase Mutant (H412N) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg452

b:3.6
occ:1.61
OE2 A:GLU322 2.2 13.2 1.0
O A:HOH456 2.2 13.0 1.0
OG1 A:THR155 2.2 9.2 1.0
OD2 A:ASP51 2.2 28.0 1.0
O A:HOH457 2.2 12.3 1.0
O A:HOH454 2.3 18.9 1.0
CG A:ASP51 3.2 29.3 1.0
CD A:GLU322 3.2 17.0 1.0
CB A:THR155 3.3 12.5 1.0
OD2 A:ASP153 3.5 27.0 1.0
OE1 A:GLU322 3.6 14.9 1.0
CB A:ASP51 3.7 19.5 1.0
N A:THR155 4.1 12.7 1.0
CG2 A:THR155 4.2 7.0 1.0
OD1 A:ASP51 4.3 30.6 1.0
CA A:THR155 4.3 12.7 1.0
O A:HOH531 4.3 19.7 1.0
CG A:GLU322 4.5 10.0 1.0
CG A:ASP153 4.6 25.7 1.0
OG A:SER102 4.6 22.5 1.0
CB A:ALA324 4.6 18.1 1.0
CB A:SER102 4.6 16.4 1.0
O A:ALA324 4.8 26.9 1.0
ZN A:ZN451 4.8 19.8 0.9
OD2 A:ASP369 4.8 13.5 1.0
CA A:ALA324 4.9 20.9 1.0
CA A:ASP51 5.0 13.9 1.0

Magnesium binding site 2 out of 2 in 1ali

Go back to Magnesium Binding Sites List in 1ali
Magnesium binding site 2 out of 2 in the Alkaline Phosphatase Mutant (H412N)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Alkaline Phosphatase Mutant (H412N) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg452

b:5.4
occ:1.37
O B:HOH525 2.2 25.9 1.0
OE2 B:GLU322 2.2 16.1 1.0
OG1 B:THR155 2.2 15.6 1.0
OD2 B:ASP51 2.2 29.7 1.0
O B:HOH524 2.3 23.9 0.8
O B:HOH526 2.3 15.8 0.8
CD B:GLU322 3.2 20.3 1.0
CG B:ASP51 3.3 29.6 1.0
CB B:THR155 3.3 17.4 1.0
OD2 B:ASP153 3.5 28.7 1.0
OE1 B:GLU322 3.5 22.1 1.0
CB B:ASP51 3.7 19.6 1.0
N B:THR155 4.1 14.4 1.0
CG2 B:THR155 4.2 11.9 1.0
OD1 B:ASP51 4.3 30.1 1.0
CA B:THR155 4.3 16.1 1.0
O B:HOH556 4.4 19.2 1.0
CG B:ASP153 4.5 26.9 1.0
CG B:GLU322 4.5 13.1 1.0
CB B:ALA324 4.6 19.9 1.0
CB B:SER102 4.7 17.8 1.0
O B:ALA324 4.7 24.0 1.0
OG B:SER102 4.8 25.3 1.0
CA B:ALA324 4.8 21.1 1.0
ZN B:ZN451 4.9 21.8 0.9
OD2 B:ASP369 4.9 11.7 1.0

Reference:

L.Ma, T.T.Tibbitts, E.R.Kantrowitz. Escherichia Coli Alkaline Phosphatase: X-Ray Structural Studies of A Mutant Enzyme (His-412-->Asn) at One of the Catalytically Important Zinc Binding Sites. Protein Sci. V. 4 1498 1995.
ISSN: ISSN 0961-8368
PubMed: 8520475
Page generated: Mon Dec 14 03:33:30 2020

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