Atomistry » Magnesium » PDB 101d-1amu » 1alj
Atomistry »
  Magnesium »
    PDB 101d-1amu »
      1alj »

Magnesium in PDB 1alj: 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: 1alj 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 / 2.60
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 194.760, 167.740, 76.230, 90.00, 90.00, 90.00
R / Rfree (%) 16.6 / n/a

Other elements in 1alj:

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

Zinc (Zn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Alkaline Phosphatase Mutant (H412N) (pdb code 1alj). 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: 1alj:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1alj

Go back to Magnesium Binding Sites List in 1alj
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:51.6
occ:1.00
O A:HOH500 2.5 69.8 1.0
OG1 A:THR155 2.7 14.2 1.0
OE2 A:GLU322 2.7 11.2 1.0
OD1 A:ASP51 2.7 91.6 1.0
O A:HOH454 2.9 50.1 0.7
OD2 A:ASP51 3.1 95.3 1.0
CG A:ASP51 3.1 80.9 1.0
O A:HOH456 3.3 75.5 0.8
OD2 A:ASP153 3.5 26.3 1.0
CB A:THR155 3.6 4.0 1.0
CD A:GLU322 3.8 2.0 1.0
N A:THR155 3.9 5.0 1.0
CB A:SER102 4.0 10.2 1.0
OG A:SER102 4.0 29.1 1.0
OE1 A:GLU322 4.2 9.1 1.0
O A:HOH524 4.2 36.8 1.0
OD2 A:ASP369 4.3 36.0 1.0
CA A:THR155 4.4 11.5 1.0
CG A:ASP153 4.4 14.9 1.0
CB A:ASP51 4.4 47.8 1.0
ZN A:ZN451 4.5 45.9 0.2
CG2 A:THR155 4.8 2.6 1.0

Magnesium binding site 2 out of 2 in 1alj

Go back to Magnesium Binding Sites List in 1alj
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:48.9
occ:0.96
OG1 B:THR155 2.5 19.1 1.0
O B:HOH519 3.0 52.4 0.8
OE2 B:GLU322 3.0 25.5 1.0
OD1 B:ASP51 3.1 81.5 1.0
O B:HOH520 3.3 74.9 0.6
OD2 B:ASP153 3.3 34.7 1.0
CB B:THR155 3.4 13.4 1.0
N B:THR155 3.4 11.0 1.0
CG B:ASP51 3.6 71.5 1.0
OD2 B:ASP51 3.7 84.0 1.0
CB B:SER102 3.8 4.5 1.0
CD B:GLU322 4.0 7.8 1.0
CA B:THR155 4.0 15.5 1.0
O B:HOH548 4.0 23.7 1.0
OG B:SER102 4.0 30.0 1.0
CG B:ASP153 4.2 23.7 1.0
OE1 B:GLU322 4.2 12.1 1.0
OD2 B:ASP369 4.4 27.8 1.0
C B:ALA154 4.4 12.9 1.0
CB B:ALA154 4.4 4.4 1.0
N B:ALA154 4.6 11.4 1.0
ZN B:ZN451 4.6 54.6 0.4
CA B:ALA154 4.6 12.6 1.0
CG2 B:THR155 4.6 14.4 1.0
OD1 B:ASP153 4.8 21.3 1.0
CD B:PRO156 4.8 9.0 1.0
CB B:ASP51 4.9 42.0 1.0
CB B:ASP153 5.0 15.3 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 03:35:07 2020

Last articles

Br in 7L32
Br in 6ZVO
Br in 6YVZ
Br in 6YVW
Br in 6TQD
Br in 6VHQ
Br in 6TU4
Br in 6VD4
Br in 6VDR
Br in 6VD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy