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Magnesium in PDB 1urb: Alkaline Phosphatase (N51MG)

Enzymatic activity of Alkaline Phosphatase (N51MG)

All present enzymatic activity of Alkaline Phosphatase (N51MG):
3.1.3.1;

Protein crystallography data

The structure of Alkaline Phosphatase (N51MG), PDB code: 1urb was solved by T.T.Tibbitts, J.E.Murphy, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.14
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 195.720, 168.480, 76.330, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 24.1

Other elements in 1urb:

The structure of Alkaline Phosphatase (N51MG) also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Alkaline Phosphatase (N51MG) (pdb code 1urb). 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 (N51MG), PDB code: 1urb:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1urb

Go back to Magnesium Binding Sites List in 1urb
Magnesium binding site 1 out of 2 in the Alkaline Phosphatase (N51MG)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Alkaline Phosphatase (N51MG) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg451

b:16.6
occ:0.71
CE1 A:HIS370 1.9 33.2 1.0
OD2 A:ASP369 2.2 30.7 1.0
OD1 A:ASN51 2.3 26.6 1.0
OG A:SER102 2.4 27.1 1.0
NE2 A:HIS370 2.6 32.1 1.0
ND1 A:HIS370 2.6 33.7 1.0
CG A:ASP369 2.8 26.0 1.0
OD1 A:ASP369 3.0 14.2 1.0
CG A:ASN51 3.3 29.1 1.0
CB A:SER102 3.3 15.8 1.0
CD2 A:HIS370 3.5 28.6 1.0
CG A:HIS370 3.5 19.8 1.0
ND2 A:ASN51 3.7 30.7 1.0
CA A:SER102 3.8 14.8 1.0
N A:SER102 4.1 10.4 1.0
CB A:ASP369 4.1 18.8 1.0
ZN A:ZN450 4.2 27.4 0.8
O4 A:PO4453 4.3 34.3 0.6
OD1 A:ASP327 4.3 28.1 1.0
N A:GLY52 4.3 10.0 1.0
CG A:ASP327 4.4 27.2 1.0
O2 A:PO4453 4.4 23.6 0.6
OD2 A:ASP327 4.6 34.4 1.0
O1 A:PO4453 4.6 31.8 0.6
CB A:ASN51 4.6 20.7 1.0
P A:PO4453 4.6 31.2 0.6
O A:HOH628 4.7 33.1 1.0
N A:HIS370 4.7 14.6 1.0
O A:HOH694 4.7 40.9 1.0
CB A:HIS370 4.8 20.3 1.0
CA A:ASN51 4.8 12.6 1.0
C A:ASP101 4.8 14.8 1.0
C A:ASN51 4.8 12.2 1.0
CB A:ASP327 4.9 28.9 1.0
NE2 A:HIS412 4.9 33.1 1.0
CA A:GLY52 4.9 12.3 1.0

Magnesium binding site 2 out of 2 in 1urb

Go back to Magnesium Binding Sites List in 1urb
Magnesium binding site 2 out of 2 in the Alkaline Phosphatase (N51MG)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Alkaline Phosphatase (N51MG) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg451

b:20.1
occ:0.59
OD1 B:ASN51 2.2 26.3 1.0
OG B:SER102 2.2 29.9 1.0
CE1 B:HIS370 2.3 27.5 1.0
OD2 B:ASP369 2.4 27.4 1.0
NE2 B:HIS370 3.0 25.3 1.0
CG B:ASN51 3.1 27.6 1.0
CB B:SER102 3.1 17.9 1.0
ND1 B:HIS370 3.1 30.4 1.0
CG B:ASP369 3.2 24.5 1.0
ND2 B:ASN51 3.3 30.6 1.0
OD1 B:ASP369 3.4 25.7 1.0
O4 B:PO4453 3.8 39.4 0.8
CA B:SER102 3.8 18.1 1.0
CG B:ASP327 4.0 33.2 1.0
CD2 B:HIS370 4.0 18.5 1.0
OD1 B:ASP327 4.0 35.9 1.0
ZN B:ZN450 4.0 36.2 0.9
OD2 B:ASP327 4.1 35.2 1.0
CG B:HIS370 4.1 22.3 1.0
O1 B:PO4453 4.1 35.5 0.8
N B:SER102 4.1 12.8 1.0
O2 B:PO4453 4.2 34.3 0.8
P B:PO4453 4.2 37.4 0.8
CB B:ASN51 4.5 18.2 1.0
N B:GLY52 4.5 11.2 1.0
O B:HOH506 4.5 55.2 1.0
CB B:ASP327 4.5 28.1 1.0
CB B:ASP369 4.5 17.2 1.0
NE2 B:HIS412 4.7 38.9 1.0
O B:HOH572 4.8 39.1 1.0
CA B:ASN51 4.8 12.7 1.0
C B:ASN51 4.8 13.6 1.0
CE1 B:HIS412 4.8 35.5 1.0

Reference:

T.T.Tibbitts, J.E.Murphy, E.R.Kantrowitz. Kinetic and Structural Consequences of Replacing the Aspartate Bridge By Asparagine in the Catalytic Metal Triad of Escherichia Coli Alkaline Phosphatase. J.Mol.Biol. V. 257 700 1996.
ISSN: ISSN 0022-2836
PubMed: 8648634
DOI: 10.1006/JMBI.1996.0195
Page generated: Mon Dec 14 06:53:32 2020

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