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Zinc in PDB 1elx: E. Coli Alkaline Phosphatase Mutant (S102A)

Enzymatic activity of E. Coli Alkaline Phosphatase Mutant (S102A)

All present enzymatic activity of E. Coli Alkaline Phosphatase Mutant (S102A):
3.1.3.1;

Protein crystallography data

The structure of E. Coli Alkaline Phosphatase Mutant (S102A), PDB code: 1elx was solved by B.Stec, M.Hehir, C.Brennan, M.Nolte, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 9.00 / 2.60
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 163.620, 163.620, 138.880, 90.00, 90.00, 120.00
R / Rfree (%) 15.8 / 20.7

Other elements in 1elx:

The structure of E. Coli Alkaline Phosphatase Mutant (S102A) also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the E. Coli Alkaline Phosphatase Mutant (S102A) (pdb code 1elx). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the E. Coli Alkaline Phosphatase Mutant (S102A), PDB code: 1elx:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1elx

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Zinc binding site 1 out of 4 in the E. Coli Alkaline Phosphatase Mutant (S102A)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of E. Coli Alkaline Phosphatase Mutant (S102A) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn450

b:2.0
occ:1.00
NE2 A:HIS412 1.8 3.5 1.0
NE2 A:HIS331 1.9 2.0 1.0
O1 A:PO4453 2.1 5.0 1.0
OD2 A:ASP327 2.3 13.8 1.0
OD1 A:ASP327 2.7 2.0 1.0
CE1 A:HIS412 2.7 6.2 1.0
O2 A:PO4453 2.8 7.5 1.0
CG A:ASP327 2.9 5.9 1.0
CD2 A:HIS331 2.9 7.2 1.0
P A:PO4453 2.9 18.6 1.0
CE1 A:HIS331 3.0 2.0 1.0
CD2 A:HIS412 3.0 3.0 1.0
O3 A:PO4453 3.9 5.1 1.0
NE2 A:HIS372 3.9 3.3 1.0
ND1 A:HIS412 3.9 2.1 1.0
ZN A:ZN451 4.0 2.0 0.9
O4 A:PO4453 4.0 2.0 1.0
ND1 A:HIS331 4.1 2.0 1.0
CG A:HIS412 4.1 7.3 1.0
CG A:HIS331 4.1 6.2 1.0
CE1 A:HIS370 4.1 2.0 1.0
O A:HOH654 4.2 13.1 1.0
NE2 A:HIS370 4.3 2.0 1.0
CB A:ASP327 4.4 3.8 1.0
CD2 A:HIS372 4.4 2.8 1.0
O A:HOH623 4.7 2.0 1.0
O A:ASP327 4.7 2.0 1.0
O A:HOH666 4.7 36.9 1.0
O A:HOH651 4.7 23.2 1.0
OD1 A:ASP51 4.8 2.0 1.0
CE1 A:HIS372 4.8 2.0 1.0
O A:HOH650 4.8 16.8 1.0
C A:ASP327 5.0 2.0 1.0

Zinc binding site 2 out of 4 in 1elx

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Zinc binding site 2 out of 4 in the E. Coli Alkaline Phosphatase Mutant (S102A)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of E. Coli Alkaline Phosphatase Mutant (S102A) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn451

b:2.0
occ:0.92
O2 A:PO4453 2.0 7.5 1.0
NE2 A:HIS370 2.0 2.0 1.0
OD2 A:ASP369 2.1 4.4 1.0
OD1 A:ASP51 2.1 2.0 1.0
CG A:ASP369 2.9 6.4 1.0
CE1 A:HIS370 2.9 2.0 1.0
OD1 A:ASP369 3.0 2.0 1.0
CD2 A:HIS370 3.1 5.8 1.0
CG A:ASP51 3.2 5.4 1.0
OD2 A:ASP327 3.3 13.8 1.0
P A:PO4453 3.4 18.6 1.0
OD2 A:ASP51 3.7 2.0 1.0
CG A:ASP327 3.8 5.9 1.0
CE1 A:HIS412 3.9 6.2 1.0
CB A:ALA102 3.9 8.5 1.0
O4 A:PO4453 3.9 2.0 1.0
O3 A:PO4453 3.9 5.1 1.0
ZN A:ZN450 4.0 2.0 1.0
CA A:ALA102 4.0 8.9 1.0
NE2 A:HIS412 4.1 3.5 1.0
ND1 A:HIS370 4.1 4.8 1.0
CG A:HIS370 4.2 2.0 1.0
N A:ALA102 4.3 4.0 1.0
CB A:ASP369 4.3 2.0 1.0
OD1 A:ASP327 4.3 2.0 1.0
N A:GLY52 4.3 2.0 1.0
O1 A:PO4453 4.4 5.0 1.0
CB A:ASP327 4.4 3.8 1.0
CB A:ASP51 4.5 3.0 1.0
C A:ASP51 4.6 2.0 1.0
O A:HOH454 4.7 5.2 1.0
ND1 A:HIS412 4.7 2.1 1.0
CA A:ASP51 4.7 2.0 1.0
C A:ASP101 4.8 2.0 1.0
CA A:GLY52 4.8 5.1 1.0

Zinc binding site 3 out of 4 in 1elx

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Zinc binding site 3 out of 4 in the E. Coli Alkaline Phosphatase Mutant (S102A)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of E. Coli Alkaline Phosphatase Mutant (S102A) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn450

b:2.0
occ:0.92
NE2 B:HIS331 1.9 11.4 1.0
O1 B:PO4453 1.9 5.5 1.0
NE2 B:HIS412 2.0 6.2 1.0
OD2 B:ASP327 2.4 4.1 1.0
OD1 B:ASP327 2.7 2.0 1.0
O2 B:PO4453 2.7 6.6 1.0
P B:PO4453 2.8 4.2 1.0
CD2 B:HIS331 2.9 12.8 1.0
CG B:ASP327 2.9 6.8 1.0
CE1 B:HIS412 3.0 8.6 1.0
CE1 B:HIS331 3.0 14.0 1.0
CD2 B:HIS412 3.1 10.9 1.0
O3 B:PO4453 3.8 2.0 1.0
NE2 B:HIS372 3.9 2.0 1.0
O4 B:PO4453 3.9 2.0 1.0
CG B:HIS331 4.1 11.6 1.0
ND1 B:HIS331 4.1 12.1 1.0
ND1 B:HIS412 4.1 6.5 1.0
ZN B:ZN451 4.2 2.0 1.0
CG B:HIS412 4.2 2.0 1.0
O B:HOH775 4.3 25.3 1.0
NE2 B:HIS370 4.3 2.0 1.0
CE1 B:HIS370 4.3 2.3 1.0
CB B:ASP327 4.4 5.3 1.0
CD2 B:HIS372 4.5 2.0 1.0
O B:HOH625 4.6 34.6 1.0
O B:HOH758 4.7 8.1 1.0
O B:ASP327 4.8 2.0 1.0
CE1 B:HIS372 4.8 2.0 1.0
OD1 B:ASP51 4.8 13.5 1.0

Zinc binding site 4 out of 4 in 1elx

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Zinc binding site 4 out of 4 in the E. Coli Alkaline Phosphatase Mutant (S102A)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of E. Coli Alkaline Phosphatase Mutant (S102A) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn451

b:2.0
occ:0.99
OD2 B:ASP369 2.0 11.6 1.0
O2 B:PO4453 2.0 6.6 1.0
OD1 B:ASP51 2.1 13.5 1.0
NE2 B:HIS370 2.1 2.0 1.0
CG B:ASP369 2.7 6.5 1.0
OD1 B:ASP369 2.7 3.4 1.0
CE1 B:HIS370 3.0 2.3 1.0
CD2 B:HIS370 3.1 6.0 1.0
CG B:ASP51 3.2 7.3 1.0
P B:PO4453 3.4 4.2 1.0
OD2 B:ASP327 3.4 4.1 1.0
OD2 B:ASP51 3.6 3.9 1.0
CB B:ALA102 3.8 6.1 1.0
O3 B:PO4453 3.9 2.0 1.0
CA B:ALA102 4.0 7.4 1.0
CG B:ASP327 4.0 6.8 1.0
O4 B:PO4453 4.0 2.0 1.0
CE1 B:HIS412 4.1 8.6 1.0
NE2 B:HIS412 4.1 6.2 1.0
ND1 B:HIS370 4.1 6.5 1.0
CB B:ASP369 4.1 2.0 1.0
CG B:HIS370 4.2 2.0 1.0
N B:ALA102 4.2 4.6 1.0
ZN B:ZN450 4.2 2.0 0.9
N B:GLY52 4.3 7.4 1.0
O1 B:PO4453 4.4 5.5 1.0
CB B:ASP51 4.4 9.6 1.0
OD1 B:ASP327 4.6 2.0 1.0
CB B:ASP327 4.6 5.3 1.0
C B:ASP51 4.6 4.7 1.0
CA B:ASP51 4.6 6.6 1.0
C B:ASP101 4.7 2.0 1.0
O B:HOH454 4.8 9.8 1.0
CA B:GLY52 4.9 3.5 1.0
ND1 B:HIS412 4.9 6.5 1.0
CD2 B:HIS412 5.0 10.9 1.0

Reference:

B.Stec, M.J.Hehir, C.Brennan, M.Nolte, E.R.Kantrowitz. Kinetic and X-Ray Structural Studies of Three Mutant E. Coli Alkaline Phosphatases: Insights Into the Catalytic Mechanism Without the Nucleophile SER102. J.Mol.Biol. V. 277 647 1998.
ISSN: ISSN 0022-2836
PubMed: 9533886
DOI: 10.1006/JMBI.1998.1635
Page generated: Wed Dec 16 02:48:23 2020

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