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Zinc 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:

Magnesium (Mg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Alkaline Phosphatase Mutant (H412N) (pdb code 1ali). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Alkaline Phosphatase Mutant (H412N), PDB code: 1ali:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1ali

Go back to Zinc Binding Sites List in 1ali
Zinc binding site 1 out of 4 in the Alkaline Phosphatase Mutant (H412N)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Alkaline Phosphatase Mutant (H412N) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn450

b:16.9
occ:0.23
OD1 A:ASP327 1.8 38.7 1.0
O1 A:PO4453 2.0 42.7 0.8
NE2 A:HIS370 2.5 16.3 1.0
CG A:ASP327 2.5 35.9 1.0
CE1 A:HIS370 2.6 18.1 1.0
ZN A:ZN451 2.6 19.8 0.9
OD2 A:ASP327 2.8 36.2 1.0
OD1 A:ASN412 3.0 24.9 1.0
P A:PO4453 3.2 42.6 0.8
OD1 A:ASP51 3.3 30.6 1.0
NE2 A:HIS331 3.3 51.0 1.0
OG A:SER102 3.4 22.5 1.0
ND2 A:ASN412 3.5 23.3 1.0
O4 A:PO4453 3.5 44.6 0.8
CG A:ASN412 3.6 20.1 1.0
O3 A:PO4453 3.7 40.0 0.8
CB A:ASP327 3.8 33.5 1.0
CD2 A:HIS370 3.8 16.1 1.0
ND1 A:HIS370 3.9 16.8 1.0
NE2 A:HIS372 4.0 35.6 1.0
CE1 A:HIS331 4.2 49.5 1.0
CD2 A:HIS372 4.2 31.7 1.0
CD2 A:HIS331 4.3 51.2 1.0
CG A:ASP51 4.3 29.3 1.0
O2 A:PO4453 4.5 41.4 0.8
CG A:HIS370 4.5 13.8 1.0
OD2 A:ASP369 4.6 13.5 1.0
OD2 A:ASP51 4.8 28.0 1.0
CB A:SER102 4.8 16.4 1.0
CA A:ASP327 4.9 32.1 1.0
N A:SER102 5.0 13.4 1.0
CB A:ASN412 5.0 19.0 1.0

Zinc binding site 2 out of 4 in 1ali

Go back to Zinc Binding Sites List in 1ali
Zinc binding site 2 out of 4 in the Alkaline Phosphatase Mutant (H412N)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Alkaline Phosphatase Mutant (H412N) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn451

b:19.8
occ:0.95
OD1 A:ASP51 1.9 30.6 1.0
NE2 A:HIS370 2.0 16.3 1.0
OD2 A:ASP369 2.1 13.5 1.0
OG A:SER102 2.2 22.5 1.0
ZN A:ZN450 2.6 16.9 0.2
CG A:ASP51 2.7 29.3 1.0
OD2 A:ASP51 2.8 28.0 1.0
CD2 A:HIS370 2.9 16.1 1.0
CG A:ASP369 3.0 14.8 1.0
CE1 A:HIS370 3.0 18.1 1.0
CB A:SER102 3.2 16.4 1.0
OD1 A:ASP369 3.2 10.5 1.0
OD1 A:ASP327 3.6 38.7 1.0
CA A:SER102 3.7 15.3 1.0
CG A:ASP327 3.9 35.9 1.0
CG A:HIS370 4.1 13.8 1.0
O1 A:PO4453 4.1 42.7 0.8
ND1 A:HIS370 4.1 16.8 1.0
N A:SER102 4.2 13.4 1.0
CB A:ASP51 4.2 19.5 1.0
OD2 A:ASP327 4.2 36.2 1.0
O4 A:PO4453 4.3 44.6 0.8
CB A:ASP369 4.3 10.1 1.0
N A:GLY52 4.4 11.0 1.0
O A:HOH531 4.4 19.7 1.0
O3 A:PO4453 4.5 40.0 0.8
O A:HOH454 4.5 18.9 1.0
CB A:ASP327 4.5 33.5 1.0
P A:PO4453 4.5 42.6 0.8
CA A:ASP51 4.7 13.9 1.0
C A:ASP51 4.8 15.3 1.0
MG A:MG452 4.8 3.6 1.6
ND2 A:ASN412 4.8 23.3 1.0
C A:ASP101 4.9 13.1 1.0

Zinc binding site 3 out of 4 in 1ali

Go back to Zinc Binding Sites List in 1ali
Zinc binding site 3 out of 4 in the Alkaline Phosphatase Mutant (H412N)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Alkaline Phosphatase Mutant (H412N) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn450

b:19.9
occ:0.20
OD1 B:ASP327 1.8 43.6 1.0
O1 B:PO4453 2.2 43.9 0.8
CG B:ASP327 2.5 40.4 1.0
NE2 B:HIS370 2.6 13.3 1.0
CE1 B:HIS370 2.6 15.8 1.0
ZN B:ZN451 2.6 21.8 0.9
OD2 B:ASP327 2.9 41.9 1.0
OD1 B:ASN412 3.1 24.6 1.0
NE2 B:HIS331 3.2 50.8 1.0
P B:PO4453 3.3 41.6 0.8
OG B:SER102 3.3 25.3 1.0
OD1 B:ASP51 3.4 30.1 1.0
ND2 B:ASN412 3.6 25.8 1.0
O4 B:PO4453 3.6 41.6 0.8
CG B:ASN412 3.7 23.4 1.0
O3 B:PO4453 3.8 35.6 0.8
CB B:ASP327 3.8 36.9 1.0
NE2 B:HIS372 3.8 38.4 1.0
ND1 B:HIS370 3.9 14.9 1.0
CD2 B:HIS370 3.9 12.9 1.0
CE1 B:HIS331 4.0 51.5 1.0
CD2 B:HIS372 4.2 29.7 1.0
CD2 B:HIS331 4.3 51.2 1.0
CG B:ASP51 4.4 29.6 1.0
CG B:HIS370 4.6 12.9 1.0
O2 B:PO4453 4.6 40.8 0.8
OD2 B:ASP369 4.7 11.7 1.0
CB B:SER102 4.7 17.8 1.0
OD2 B:ASP51 4.8 29.7 1.0
CA B:ASP327 4.9 32.5 1.0
CE1 B:HIS372 4.9 35.6 1.0
N B:SER102 5.0 10.0 1.0

Zinc binding site 4 out of 4 in 1ali

Go back to Zinc Binding Sites List in 1ali
Zinc binding site 4 out of 4 in the Alkaline Phosphatase Mutant (H412N)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Alkaline Phosphatase Mutant (H412N) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn451

b:21.8
occ:0.89
OD1 B:ASP51 1.9 30.1 1.0
NE2 B:HIS370 2.0 13.3 1.0
OD2 B:ASP369 2.1 11.7 1.0
OG B:SER102 2.3 25.3 1.0
ZN B:ZN450 2.6 19.9 0.2
CG B:ASP51 2.7 29.6 1.0
OD2 B:ASP51 2.9 29.7 1.0
CD2 B:HIS370 2.9 12.9 1.0
CG B:ASP369 2.9 16.4 1.0
CE1 B:HIS370 3.0 15.8 1.0
CB B:SER102 3.1 17.8 1.0
OD1 B:ASP369 3.2 15.4 1.0
OD1 B:ASP327 3.6 43.6 1.0
CA B:SER102 3.7 14.5 1.0
CG B:ASP327 3.9 40.4 1.0
CG B:HIS370 4.1 12.9 1.0
ND1 B:HIS370 4.1 14.9 1.0
N B:SER102 4.2 10.0 1.0
CB B:ASP51 4.2 19.6 1.0
O1 B:PO4453 4.2 43.9 0.8
OD2 B:ASP327 4.2 41.9 1.0
O B:HOH556 4.3 19.2 1.0
CB B:ASP369 4.3 10.5 1.0
O4 B:PO4453 4.4 41.6 0.8
N B:GLY52 4.4 10.9 1.0
O B:HOH524 4.4 23.9 0.8
O3 B:PO4453 4.5 35.6 0.8
CB B:ASP327 4.5 36.9 1.0
P B:PO4453 4.6 41.6 0.8
CA B:ASP51 4.7 14.3 1.0
C B:ASP51 4.8 14.0 1.0
MG B:MG452 4.9 5.4 1.4
C B:ASP101 4.9 13.7 1.0
ND2 B:ASN412 4.9 25.8 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: Wed Dec 16 02:44:53 2020

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