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Zinc 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:

Magnesium (Mg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Alkaline Phosphatase (N51MG) (pdb code 1urb). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Alkaline Phosphatase (N51MG), PDB code: 1urb:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1urb

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


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Alkaline Phosphatase (N51MG) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn450

b:27.4
occ:0.84
NE2 A:HIS412 1.8 33.1 1.0
O1 A:PO4453 1.9 31.8 0.6
OD1 A:ASP327 2.1 28.1 1.0
NE2 A:HIS331 2.3 34.8 1.0
OD2 A:ASP327 2.6 34.4 1.0
CE1 A:HIS412 2.7 32.5 1.0
CG A:ASP327 2.7 27.2 1.0
CD2 A:HIS412 3.0 33.4 1.0
CD2 A:HIS331 3.2 28.7 1.0
P A:PO4453 3.2 31.2 0.6
NE2 A:HIS370 3.3 32.1 1.0
CE1 A:HIS331 3.3 26.6 1.0
CE1 A:HIS370 3.6 33.2 1.0
NE2 A:HIS372 3.6 29.5 1.0
O2 A:PO4453 3.7 23.6 0.6
O4 A:PO4453 3.8 34.3 0.6
ND1 A:HIS412 3.9 32.1 1.0
CG A:HIS412 4.0 32.2 1.0
MG A:MG451 4.2 16.6 0.7
CB A:ASP327 4.2 28.9 1.0
CD2 A:HIS372 4.2 26.1 1.0
O3 A:PO4453 4.3 36.2 0.6
CG A:HIS331 4.4 28.8 1.0
ND1 A:HIS331 4.4 26.1 1.0
OG A:SER102 4.5 27.1 1.0
CD2 A:HIS370 4.5 28.6 1.0
CE1 A:HIS372 4.6 33.5 1.0
OD1 A:ASN51 4.6 26.6 1.0
ND1 A:HIS370 4.8 33.7 1.0
O A:ASP327 4.9 16.5 1.0

Zinc binding site 2 out of 2 in 1urb

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


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Alkaline Phosphatase (N51MG) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn450

b:36.2
occ:0.88
O1 B:PO4453 1.9 35.5 0.8
NE2 B:HIS412 1.9 38.9 1.0
OD1 B:ASP327 2.0 35.9 1.0
NE2 B:HIS331 2.1 36.6 1.0
CG B:ASP327 2.6 33.2 1.0
OD2 B:ASP327 2.7 35.2 1.0
CE1 B:HIS412 2.8 35.5 1.0
CD2 B:HIS331 2.9 37.3 1.0
CD2 B:HIS412 3.1 35.7 1.0
CE1 B:HIS331 3.2 31.4 1.0
P B:PO4453 3.3 37.4 0.8
NE2 B:HIS370 3.4 25.3 1.0
NE2 B:HIS372 3.5 38.1 1.0
CE1 B:HIS370 3.7 27.5 1.0
O2 B:PO4453 3.9 34.3 0.8
O4 B:PO4453 3.9 39.4 0.8
ND1 B:HIS412 4.0 34.0 1.0
MG B:MG451 4.0 20.1 0.6
CG B:HIS331 4.1 34.0 1.0
CB B:ASP327 4.1 28.1 1.0
CD2 B:HIS372 4.1 30.5 1.0
CG B:HIS412 4.2 34.3 1.0
ND1 B:HIS331 4.2 31.6 1.0
O3 B:PO4453 4.2 41.9 0.8
CE1 B:HIS372 4.4 34.2 1.0
O B:ASP327 4.6 19.1 1.0
CD2 B:HIS370 4.6 18.5 1.0
OG B:SER102 4.7 29.9 1.0
OD1 B:ASN51 4.9 26.3 1.0
C B:ASP327 4.9 27.2 1.0
CA B:ASP327 5.0 24.1 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: Wed Dec 16 03:06:58 2020

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