Chlorine in PDB 4ob6: Complex Structure of Esterase Rppe S159A/W187H and Substrate (S)-Ac- Cpa

The structure of Complex Structure of Esterase Rppe S159A/W187H and Substrate (S)-Ac- Cpa, PDB code: 4ob6 was solved by S.Dou, X.D.Kong, B.D.Ma, Q.Chen, J.H.Zhou, J.H.Xu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.74 / 1.70
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	95.438, 95.438, 88.297, 90.00, 90.00, 90.00
R / Rfree (%)	16.4 / 18.1

The binding sites of Chlorine atom in the Complex Structure of Esterase Rppe S159A/W187H and Substrate (S)-Ac- Cpa (pdb code 4ob6). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Complex Structure of Esterase Rppe S159A/W187H and Substrate (S)-Ac- Cpa, PDB code: 4ob6:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Complex Structure of Esterase Rppe S159A/W187H and Substrate (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 Complex Structure of Esterase Rppe S159A/W187H and Substrate (S)-Ac- Cpa within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:34.4 occ:0.72 CL A:S2T401 0.0 34.4 0.7 C06 A:S2T401 1.7 31.6 0.7 C01 A:S2T401 2.7 35.6 0.7 C05 A:S2T401 2.7 28.8 0.7 C07 A:S2T401 3.2 31.5 0.7 C09 A:S2T401 3.3 28.4 0.7 CA A:GLY87 3.5 20.6 1.0 O14 A:S2T401 3.6 35.0 0.7 CD2 A:LEU36 3.7 21.6 1.0 O15 A:S2T401 3.8 29.2 0.7 CD1 A:LEU36 3.9 21.5 1.0 CD2 A:LEU290 3.9 20.2 1.0 C02 A:S2T401 4.0 31.4 0.7 C04 A:S2T401 4.0 30.9 0.7 N A:GLY87 4.1 18.0 1.0 CG A:LEU36 4.3 20.2 1.0 CD1 A:LEU91 4.4 31.9 1.0 C03 A:S2T401 4.5 32.4 0.7 O08 A:S2T401 4.6 33.8 0.7 C A:GLY87 4.6 21.4 1.0 CB A:LEU91 4.8 21.0 1.0 C A:GLY86 4.9 18.6 1.0 CB A:LEU36 4.9 17.7 1.0 O A:GLY87 5.0 19.8 1.0

Chlorine binding site 2 out of 3 in the Complex Structure of Esterase Rppe S159A/W187H and Substrate (S)-Ac- Cpa


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Complex Structure of Esterase Rppe S159A/W187H and Substrate (S)-Ac- Cpa within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:38.8 occ:1.00 CL A:S2T402 0.0 38.8 1.0 C06 A:S2T402 1.8 37.3 1.0 C01 A:S2T402 2.7 32.6 1.0 O08 A:S2T402 2.7 53.6 1.0 C05 A:S2T402 2.8 38.0 1.0 C07 A:S2T402 3.3 43.8 1.0 C10 A:S2T402 3.8 46.5 1.0 C01 A:S2T401 3.9 35.6 0.7 CD1 A:LEU36 3.9 21.5 1.0 CA A:LEU36 3.9 16.6 1.0 C02 A:S2T402 4.0 35.9 1.0 C04 A:S2T402 4.1 36.7 1.0 C12 A:S2T402 4.1 43.0 1.0 CE1 A:PHE207 4.1 31.4 1.0 CB A:LEU36 4.2 17.7 1.0 CG1 A:VAL35 4.2 26.0 1.0 CZ A:PHE207 4.3 29.4 1.0 N A:LEU36 4.3 21.0 1.0 C02 A:S2T401 4.3 31.4 0.7 C09 A:S2T402 4.4 47.7 1.0 C03 A:S2T402 4.5 33.2 1.0 O A:VAL35 4.6 21.6 1.0 C A:VAL35 4.6 23.2 1.0 CB A:ALA39 4.7 21.1 1.0 CG A:LEU36 4.7 20.2 1.0 O15 A:S2T402 4.7 42.2 1.0 O11 A:S2T402 4.9 60.5 1.0 C06 A:S2T401 4.9 31.6 0.7

Chlorine binding site 3 out of 3 in the Complex Structure of Esterase Rppe S159A/W187H and Substrate (S)-Ac- Cpa


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Complex Structure of Esterase Rppe S159A/W187H and Substrate (S)-Ac- Cpa within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl403 b:38.8 occ:1.00 CL A:S2T403 0.0 38.8 1.0 C06 A:S2T403 1.7 37.2 1.0 C01 A:S2T403 2.7 35.8 1.0 C05 A:S2T403 2.8 28.1 1.0 O08 A:S2T403 3.0 45.5 1.0 C07 A:S2T403 3.3 37.9 1.0 CE1 A:HIS314 3.8 22.9 1.0 C02 A:S2T403 4.0 31.6 1.0 C04 A:S2T403 4.1 34.5 1.0 C10 A:S2T403 4.1 41.0 1.0 CG2 A:THR275 4.2 19.5 1.0 C09 A:S2T403 4.3 29.3 1.0 O15 A:S2T403 4.3 29.9 1.0 C03 A:S2T403 4.5 32.8 1.0 ND1 A:HIS314 4.6 24.3 1.0 O11 A:S2T403 4.7 45.8 1.0 NE2 A:HIS314 4.8 22.4 1.0 CG A:PRO247 4.8 20.3 1.0 OG1 A:THR275 4.9 20.4 1.0 CB A:THR275 4.9 20.9 1.0 C12 A:S2T403 4.9 41.3 1.0 CB A:PRO247 5.0 19.9 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