Chlorine in PDB 5ct4: Wild-Type Bacillus Subtilis Lipase A with 5% [Bmim][Cl]

All present enzymatic activity of Wild-Type Bacillus Subtilis Lipase A with 5% [Bmim][Cl]:
3.1.1.3;

The structure of Wild-Type Bacillus Subtilis Lipase A with 5% [Bmim][Cl], PDB code: 5ct4 was solved by E.M.Nordwald, J.G.Plaks, J.R.Snell, M.C.Sousa, J.L.Kaar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.40 / 1.49
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	39.440, 83.160, 95.820, 90.00, 90.00, 90.00
R / Rfree (%)	12.6 / 15.6

The binding sites of Chlorine atom in the Wild-Type Bacillus Subtilis Lipase A with 5% [Bmim][Cl] (pdb code 5ct4). 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 Wild-Type Bacillus Subtilis Lipase A with 5% [Bmim][Cl], PDB code: 5ct4:

Chlorine binding site 1 out of 1 in the Wild-Type Bacillus Subtilis Lipase A with 5% [Bmim][Cl]


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Wild-Type Bacillus Subtilis Lipase A with 5% [Bmim][Cl] within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl204 b:14.6 occ:1.00 H A:HIS156 2.4 12.8 1.0 H2 A:HOH443 2.4 22.8 1.0 H A:MET134 2.4 12.1 1.0 H2 A:HOH526 2.5 32.5 1.0 H2 A:HOH334 2.7 22.6 1.0 H1 A:HOH334 2.7 22.6 1.0 HG3 A:MET134 2.9 16.2 0.4 HB2 A:MET134 3.1 14.3 0.6 HG12 A:ILE135 3.1 18.6 1.0 O A:HOH334 3.1 18.9 1.0 HB2 A:HIS156 3.2 11.7 1.0 HB2 A:MET134 3.2 15.9 0.4 O A:HOH443 3.2 19.0 1.0 O A:HOH526 3.2 27.1 1.0 N A:HIS156 3.3 10.7 1.0 N A:MET134 3.3 10.1 1.0 H1 A:HOH526 3.4 32.5 1.0 HG2 A:MET134 3.5 13.2 0.6 HA A:ASP133 3.5 10.0 1.0 HB3 A:HIS156 3.5 11.7 1.0 HA2 A:GLY155 3.6 13.4 1.0 CG A:MET134 3.6 13.5 0.4 H1 A:HOH443 3.7 22.8 1.0 CB A:HIS156 3.7 9.8 1.0 CB A:MET134 3.7 13.3 0.4 CB A:MET134 3.8 11.9 0.6 HA3 A:GLY155 3.8 13.4 1.0 H2 A:HOH446 4.0 23.6 1.0 CA A:MET134 4.0 11.2 0.4 CA A:MET134 4.0 10.7 0.6 H A:ILE135 4.0 13.4 1.0 CA A:GLY155 4.0 11.2 1.0 CG1 A:ILE135 4.0 15.5 1.0 O A:ALA132 4.1 10.8 1.0 CG A:MET134 4.1 11.0 0.6 CA A:HIS156 4.1 10.8 1.0 C A:GLY155 4.1 10.3 1.0 C A:ASP133 4.3 8.8 1.0 CA A:ASP133 4.3 8.4 1.0 HG13 A:ILE135 4.3 18.6 1.0 N A:ILE135 4.3 11.2 1.0 HG2 A:MET134 4.4 16.2 0.4 HG3 A:MET134 4.5 13.2 0.6 OD1 A:ASP133 4.5 8.2 1.0 C A:MET134 4.5 12.3 1.0 SD A:MET134 4.5 14.6 0.4 HD11 A:ILE135 4.5 21.5 1.0 H A:ILE157 4.5 16.2 1.0 HB3 A:MET134 4.6 14.3 0.6 HB3 A:MET134 4.6 15.9 0.4 HA A:HIS156 4.7 12.9 1.0 H2 A:HOH525 4.7 42.5 1.0 CD1 A:ILE135 4.7 18.0 1.0 HB A:ILE135 4.7 14.8 1.0 HD13 A:ILE135 4.8 21.5 1.0 O A:HOH446 4.8 19.7 1.0 H1 A:HOH446 4.8 23.6 1.0 HA A:MET134 4.9 13.5 0.4 CB A:ILE135 4.9 12.4 1.0

E.M.Nordwald, J.G.Plaks, J.R.Snell, M.C.Sousa, J.L.Kaar. Crystallographic Investigation of Imidazolium Ionic Liquid Effects on Enzyme Structure. Chembiochem V. 16 2456 2015.
ISSN: ESSN 1439-7633
PubMed: 26388426
DOI: 10.1002/CBIC.201500398