Chlorine in PDB 5tic: X-Ray Structure of Wild-Type E. Coli Acyl-Coa Thioesterase I at pH 5

All present enzymatic activity of X-Ray Structure of Wild-Type E. Coli Acyl-Coa Thioesterase I at pH 5:
3.1.1.5;

The structure of X-Ray Structure of Wild-Type E. Coli Acyl-Coa Thioesterase I at pH 5, PDB code: 5tic was solved by J.B.Thoden, H.M.Holden, M.J.Grisewood, N.J.Hernandez Lozada, N.P.Gifford, D.Mendez-Perez, H.A.Schoenberger, M.F.Allan, B.F.Pfleger, C.D.Marines, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.65
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	40.922, 82.124, 53.903, 90.00, 90.44, 90.00
R / Rfree (%)	18.6 / 22.2

The binding sites of Chlorine atom in the X-Ray Structure of Wild-Type E. Coli Acyl-Coa Thioesterase I at pH 5 (pdb code 5tic). 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 X-Ray Structure of Wild-Type E. Coli Acyl-Coa Thioesterase I at pH 5, PDB code: 5tic:

Chlorine binding site 1 out of 1 in the X-Ray Structure of Wild-Type E. Coli Acyl-Coa Thioesterase I at pH 5


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of X-Ray Structure of Wild-Type E. Coli Acyl-Coa Thioesterase I at pH 5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:32.3 occ:1.00 O A:HOH454 3.3 25.4 1.0 N A:PHE139 3.3 10.9 1.0 NH2 A:ARG108 3.4 29.6 1.0 NE A:ARG108 3.6 22.4 1.0 CA A:PRO138 3.9 12.6 1.0 CB A:PHE139 3.9 11.2 1.0 CB A:PRO138 3.9 16.1 1.0 CG A:GLN106 3.9 9.3 1.0 CZ A:ARG108 4.0 25.7 1.0 C A:PRO138 4.1 10.6 1.0 CA A:PHE139 4.2 10.9 1.0 CB A:GLN106 4.3 8.5 1.0 O A:HOH342 4.5 16.9 1.0 O A:PHE139 4.6 13.3 1.0 CG A:GLU142 4.6 21.8 1.0 CD A:ARG108 4.8 19.3 1.0 C A:PHE139 4.9 12.4 1.0

M.J.Grisewood, N.J.Hernandez Lozada, J.B.Thoden, N.P.Gifford, D.Mendez-Perez, H.A.Schoenberger, M.F.Allan, M.E.Floy, R.Y.Lai, H.M.Holden, B.F.Pfleger, C.D.Maranas. Computational Redesign of Acyl-Acp Thioesterase with Improved Selectivity Toward Medium-Chain-Length Fatty Acids. Acs Catal V. 7 3837 2017.
ISSN: ESSN 2155-5435
PubMed: 29375928
DOI: 10.1021/ACSCATAL.7B00408