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Fluorine in PDB 4izt: The E41Q Mutant of the Amidase From Nesterenkonia Sp. AN1 Showing Covalent Addition of the Acetamide Moiety of Fluoroacetamide at the Active Site Cysteine

Enzymatic activity of The E41Q Mutant of the Amidase From Nesterenkonia Sp. AN1 Showing Covalent Addition of the Acetamide Moiety of Fluoroacetamide at the Active Site Cysteine

All present enzymatic activity of The E41Q Mutant of the Amidase From Nesterenkonia Sp. AN1 Showing Covalent Addition of the Acetamide Moiety of Fluoroacetamide at the Active Site Cysteine:
3.5.1.4;

Protein crystallography data

The structure of The E41Q Mutant of the Amidase From Nesterenkonia Sp. AN1 Showing Covalent Addition of the Acetamide Moiety of Fluoroacetamide at the Active Site Cysteine, PDB code: 4izt was solved by S.W.Kimani, B.T.Sewell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.47 / 1.92
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 76.580, 115.450, 64.930, 90.00, 90.00, 90.00
R / Rfree (%) 14.5 / 18.2

Fluorine Binding Sites:

The binding sites of Fluorine atom in the The E41Q Mutant of the Amidase From Nesterenkonia Sp. AN1 Showing Covalent Addition of the Acetamide Moiety of Fluoroacetamide at the Active Site Cysteine (pdb code 4izt). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the The E41Q Mutant of the Amidase From Nesterenkonia Sp. AN1 Showing Covalent Addition of the Acetamide Moiety of Fluoroacetamide at the Active Site Cysteine, PDB code: 4izt:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in 4izt

Go back to Fluorine Binding Sites List in 4izt
Fluorine binding site 1 out of 2 in the The E41Q Mutant of the Amidase From Nesterenkonia Sp. AN1 Showing Covalent Addition of the Acetamide Moiety of Fluoroacetamide at the Active Site Cysteine


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of The E41Q Mutant of the Amidase From Nesterenkonia Sp. AN1 Showing Covalent Addition of the Acetamide Moiety of Fluoroacetamide at the Active Site Cysteine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F302

b:42.1
occ:1.00
F A:FTM302 0.0 42.1 1.0
C2 A:FTM302 1.4 37.1 1.0
C1 A:FTM302 2.4 36.4 1.0
O A:FTM302 3.1 38.1 1.0
OE1 A:GLU149 3.2 13.4 1.0
N A:FTM302 3.3 33.8 1.0
CG2 A:VAL178 3.9 11.2 1.0
CD A:GLU149 4.0 14.8 1.0
OE2 A:GLU149 4.0 15.8 1.0
OE2 A:GLU175 4.0 38.4 1.0
CD A:GLU175 4.1 38.4 1.0
CG A:GLU175 4.4 33.7 1.0
OE1 A:GLU175 4.6 41.6 1.0
CB A:GLU175 4.6 24.4 1.0
CD1 A:LEU171 4.7 22.6 1.0
CE1 A:TYR115 4.9 22.0 1.0

Fluorine binding site 2 out of 2 in 4izt

Go back to Fluorine Binding Sites List in 4izt
Fluorine binding site 2 out of 2 in the The E41Q Mutant of the Amidase From Nesterenkonia Sp. AN1 Showing Covalent Addition of the Acetamide Moiety of Fluoroacetamide at the Active Site Cysteine


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of The E41Q Mutant of the Amidase From Nesterenkonia Sp. AN1 Showing Covalent Addition of the Acetamide Moiety of Fluoroacetamide at the Active Site Cysteine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F303

b:44.4
occ:0.80
F A:FTM303 0.0 44.4 0.8
C2 A:FTM303 1.4 41.8 1.0
C1 A:FTM303 2.3 43.5 1.0
O A:FTM303 2.6 41.5 1.0
O A:ALA170 2.7 16.7 1.0
N A:ACM301 3.0 29.0 1.0
C2 A:ACM301 3.3 32.3 1.0
N A:FTM303 3.5 43.7 1.0
C1 A:ACM301 3.6 27.1 1.0
OH A:TYR47 3.7 16.0 1.0
CZ A:TYR47 3.9 15.8 1.0
C A:ALA170 4.0 15.1 1.0
CE2 A:TYR47 4.0 14.6 1.0
CD2 A:TYR115 4.4 19.3 1.0
SG A:CYS145 4.6 17.0 0.9
CE1 A:TYR47 4.6 11.3 1.0
CA A:LEU171 4.7 14.2 1.0
CB A:ALA170 4.7 12.5 1.0
CE2 A:TYR115 4.8 22.5 1.0
O A:FTM302 4.8 38.1 1.0
N A:LEU171 4.8 11.5 1.0
O A:ACM301 4.8 20.8 1.0
CD2 A:TYR47 4.8 10.0 1.0
OE2 A:GLU119 4.9 26.2 1.0
N A:ALA172 5.0 14.8 1.0
CA A:ALA170 5.0 11.6 1.0

Reference:

S.W.Kimani, R.Hunter, M.Vlok, J.Watermeyer, B.T.Sewell. Covalent Modifications of the Active Site Cysteine Occur As A Result of Mutating the Glutamate of the Catalytic Triad in the Amidase From Nesterenkonia Sp. To Be Published.
Page generated: Sun Dec 13 12:04:57 2020

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