Chlorine in PDB 4ou4: Crystal Structure of Esterase Rppe Mutant S159A Complexed with (S)-Ac- Cpa

All present enzymatic activity of Crystal Structure of Esterase Rppe Mutant S159A Complexed with (S)-Ac- Cpa:
3.1.1.1;

The structure of Crystal Structure of Esterase Rppe Mutant S159A Complexed with (S)-Ac- Cpa, PDB code: 4ou4 was solved by S.Dou, X.D.Kong, B.D.Ma, J.H.Xu, J.H.Zhou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.32 / 2.40
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	94.624, 94.624, 88.533, 90.00, 90.00, 90.00
R / Rfree (%)	16.7 / 23.4

The binding sites of Chlorine atom in the Crystal Structure of Esterase Rppe Mutant S159A Complexed with (S)-Ac- Cpa (pdb code 4ou4). 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 Crystal Structure of Esterase Rppe Mutant S159A Complexed with (S)-Ac- Cpa, PDB code: 4ou4:

Chlorine binding site 1 out of 1 in the Crystal Structure of Esterase Rppe Mutant S159A Complexed with (S)-Ac- Cpa


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Esterase Rppe Mutant S159A Complexed with (S)-Ac- Cpa within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:74.0 occ:1.00 CL A:S2T401 0.0 74.0 1.0 C06 A:S2T401 1.8 69.1 1.0 C01 A:S2T401 2.7 68.9 1.0 C05 A:S2T401 2.8 50.4 1.0 C09 A:S2T401 3.1 44.5 1.0 O15 A:S2T401 3.1 40.6 1.0 C07 A:S2T401 3.2 50.2 1.0 O08 A:S2T401 3.6 53.1 1.0 O14 A:S2T401 3.6 30.8 1.0 C02 A:S2T401 4.0 63.5 1.0 C04 A:S2T401 4.0 38.0 1.0 C10 A:S2T401 4.4 59.8 1.0 C12 A:S2T401 4.5 66.1 1.0 C03 A:S2T401 4.5 40.4 1.0

S.Dou, X.D.Kong, B.D.Ma, Q.Chen, J.Zhang, J.H.Zhou, J.H.Xu. Crystal Structures of Pseudomonas Putida Esterase Reveal the Functional Role of Residues 187 and 287 in Substrate Binding and Chiral Recognition Biochem.Biophys.Res.Commun. V. 446 1145 2014.
ISSN: ISSN 0006-291X
PubMed: 24680822
DOI: 10.1016/J.BBRC.2014.03.072