Chlorine in PDB 5ny7: A C145A Mutant of Nesterenkonia AN1 Amidase Bound to Nicotinamide

All present enzymatic activity of A C145A Mutant of Nesterenkonia AN1 Amidase Bound to Nicotinamide:
3.5.1.4;

The structure of A C145A Mutant of Nesterenkonia AN1 Amidase Bound to Nicotinamide, PDB code: 5ny7 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)	30.24 / 1.31
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	75.249, 114.779, 65.363, 90.00, 90.00, 90.00
R / Rfree (%)	15.1 / 17.4

The binding sites of Chlorine atom in the A C145A Mutant of Nesterenkonia AN1 Amidase Bound to Nicotinamide (pdb code 5ny7). 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 A C145A Mutant of Nesterenkonia AN1 Amidase Bound to Nicotinamide, PDB code: 5ny7:

Chlorine binding site 1 out of 1 in the A C145A Mutant of Nesterenkonia AN1 Amidase Bound to Nicotinamide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of A C145A Mutant of Nesterenkonia AN1 Amidase Bound to Nicotinamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:23.7 occ:1.00 N A:ALA218 3.1 12.2 1.0 N A:GLN220 3.2 12.4 1.0 C A:GLY216 3.3 10.7 1.0 CB A:ALA218 3.4 14.4 1.0 CB A:GLN220 3.4 17.0 1.0 CA A:GLY216 3.5 11.2 1.0 CA A:ALA218 3.5 12.3 1.0 N A:GLY219 3.5 11.4 1.0 O A:GLY216 3.6 10.5 1.0 O A:HOH577 3.6 35.2 1.0 C A:ALA218 3.6 12.1 1.0 O A:GLN220 3.7 14.0 1.0 N A:PRO217 3.7 12.0 1.0 CG A:GLN220 3.8 25.0 1.0 N A:GLY216 3.8 10.1 1.0 CA A:GLN220 3.8 14.1 1.0 C A:GLN220 4.2 12.1 1.0 C A:PRO217 4.2 12.8 1.0 C A:GLY219 4.2 12.4 1.0 CD A:PRO217 4.3 14.1 1.0 CA A:GLY219 4.4 11.8 1.0 CD2 A:LEU222 4.4 22.6 1.0 O A:ALA218 4.4 14.2 1.0 CA A:PRO217 4.5 12.9 1.0 O A:HOH603 4.7 31.1 1.0

S.W.Kimani, G.A.Venter, B.T.Sewell. Substrate Recognition By An Amidase of the Nitrilase Superfamily To Be Published.