Chlorine in PDB 4gyn: The E142L Mutant of the Amidase From Geobacillus Pallidus

All present enzymatic activity of The E142L Mutant of the Amidase From Geobacillus Pallidus:
3.5.1.4;

The structure of The E142L Mutant of the Amidase From Geobacillus Pallidus, PDB code: 4gyn 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)	53.39 / 1.90
Space group	P 42 3 2
Cell size a, b, c (Å), α, β, γ (°)	130.789, 130.789, 130.789, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 22.5

The binding sites of Chlorine atom in the The E142L Mutant of the Amidase From Geobacillus Pallidus (pdb code 4gyn). 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, PDB code: 4gyn:

Chlorine binding site 1 out of 1 in the The E142L Mutant of the Amidase From Geobacillus Pallidus


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:30.9 occ:1.00 N A:TRP138 2.8 13.1 1.0 O A:HOH701 2.8 15.5 1.0 NZ A:LYS134 2.9 16.2 1.0 CD1 A:TRP144 3.3 14.7 1.0 OH A:TYR60 3.5 12.8 1.0 CA A:PRO137 3.6 13.3 1.0 CB A:TRP138 3.6 13.9 1.0 C A:PRO137 3.6 14.5 1.0 CB A:LEU142 3.7 21.6 1.0 CA A:TRP138 3.7 13.2 1.0 CB A:PRO137 3.8 12.6 1.0 NE1 A:TRP144 3.8 14.7 1.0 CE A:LYS134 3.9 15.7 1.0 CD A:LYS134 4.0 13.0 1.0 ND2 A:ASN117 4.0 11.3 1.0 CD1 A:LEU142 4.2 28.0 1.0 OE2 A:GLU59 4.3 11.3 1.0 C A:TRP138 4.5 13.8 1.0 CG A:TRP144 4.5 13.5 1.0 CG A:LEU142 4.6 25.4 1.0 O A:TRP138 4.8 14.6 1.0 CZ A:TYR60 4.8 13.2 1.0 O A:PRO137 4.8 17.4 1.0 CA A:LEU142 4.9 19.8 1.0 C A:LEU142 4.9 18.3 1.0 N A:PRO137 5.0 11.9 1.0

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