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Chlorine in PDB 4gyl: The E142L Mutant of the Amidase From Geobacillus Pallidus Showing the Result of Michael Addition of Acrylamide at the Active Site Cysteine

Enzymatic activity of The E142L Mutant of the Amidase From Geobacillus Pallidus Showing the Result of Michael Addition of Acrylamide at the Active Site Cysteine

All present enzymatic activity of The E142L Mutant of the Amidase From Geobacillus Pallidus Showing the Result of Michael Addition of Acrylamide at the Active Site Cysteine:
3.5.1.4;

Protein crystallography data

The structure of The E142L Mutant of the Amidase From Geobacillus Pallidus Showing the Result of Michael Addition of Acrylamide at the Active Site Cysteine, PDB code: 4gyl was solved by B.W.Weber, B.T.Sewell, S.W.Kimani, A.Varsani, D.A.Cowan, R.Hunter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.23 / 1.90
Space group P 42 3 2
Cell size a, b, c (Å), α, β, γ (°) 130.490, 130.490, 130.490, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 18.7

Chlorine Binding Sites:

The binding sites of Chlorine atom in the The E142L Mutant of the Amidase From Geobacillus Pallidus Showing the Result of Michael Addition of Acrylamide at the Active Site Cysteine (pdb code 4gyl). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the The E142L Mutant of the Amidase From Geobacillus Pallidus Showing the Result of Michael Addition of Acrylamide at the Active Site Cysteine, PDB code: 4gyl:

Chlorine binding site 1 out of 1 in 4gyl

Go back to Chlorine Binding Sites List in 4gyl
Chlorine binding site 1 out of 1 in the The E142L Mutant of the Amidase From Geobacillus Pallidus Showing the Result of Michael Addition of Acrylamide at the Active Site Cysteine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The E142L Mutant of the Amidase From Geobacillus Pallidus Showing the Result of Michael Addition of Acrylamide at the Active Site Cysteine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl402

b:37.1
occ:1.00
 N A:TRP138 2.9 14.1 1.0
ND2 A:ROP401 2.9 25.1 1.0
NZ A:LYS134 3.1 31.8 1.0
CD1 A:TRP144 3.3 17.0 1.0
OH A:TYR60 3.4 15.6 1.0
CB A:LEU142 3.6 24.1 1.0
CB A:TRP138 3.6 15.6 1.0
CG A:ROP401 3.6 24.4 1.0
OD1 A:ROP401 3.7 31.1 1.0
CA A:PRO137 3.7 14.7 1.0
C A:PRO137 3.7 14.4 1.0
CA A:TRP138 3.8 15.0 1.0
NE1 A:TRP144 3.8 15.8 1.0
CD1 A:LEU142 4.0 32.9 1.0
CE A:LYS134 4.0 24.6 1.0
CB A:PRO137 4.0 14.9 1.0
CD A:LYS134 4.1 20.0 1.0
ND2 A:ASN117 4.2 15.2 1.0
OE1 A:GLU59 4.2 12.7 1.0
CG A:LEU142 4.4 29.0 1.0
CG A:TRP144 4.5 15.7 1.0
C A:TRP138 4.5 15.8 1.0
CZ A:TYR60 4.7 16.5 1.0
O A:TRP138 4.8 16.5 1.0
CA A:LEU142 4.8 21.6 1.0
CB A:ROP401 4.9 19.3 1.0
C A:LEU142 4.9 20.2 1.0
O A:PRO137 5.0 15.7 1.0
O A:LEU142 5.0 22.7 1.0

Reference:

B.W.Weber, S.W.Kimani, A.Varsani, D.A.Cowan, R.Hunter, G.A.Venter, J.C.Gumbart, B.T.Sewell. The Mechanism of the Amidases: Mutating the Glutamate Adjacent to the Catalytic Triad Inactivates the Enzyme Due to Substrate Mispositioning. J.Biol.Chem. V. 288 28514 2013.
ISSN: ISSN 0021-9258
PubMed: 23946488
DOI: 10.1074/JBC.M113.503284
Page generated: Sat Dec 12 10:41:05 2020

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