Chlorine in PDB 5frd: Structure of A Thermophilic Esterase

All present enzymatic activity of Structure of A Thermophilic Esterase:
3.1.1.1;

The structure of Structure of A Thermophilic Esterase, PDB code: 5frd was solved by C.Sayer, W.Finnigan, M.N.Isupov, M.Levisson, S.W.M.Kengen, J.Van Der Oost, N.Harmer, J.A.Littlechild, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	70.29 / 1.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.070, 67.200, 140.570, 90.00, 90.00, 90.00
R / Rfree (%)	15.649 / 17.347

The binding sites of Chlorine atom in the Structure of A Thermophilic Esterase (pdb code 5frd). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of A Thermophilic Esterase, PDB code: 5frd:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structure of A Thermophilic Esterase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of A Thermophilic Esterase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1258 b:16.7 occ:1.00 OG A:SER30 3.0 15.5 1.0 OG A:SER89 3.1 19.0 1.0 O A:HOH2127 3.2 23.1 1.0 N A:SER30 3.2 12.6 1.0 N A:LEU90 3.3 14.6 1.0 CB A:SER30 3.3 13.1 1.0 CB A:SER89 3.4 16.9 1.0 CB A:LEU90 3.7 15.7 0.3 CB A:LEU90 3.7 15.3 0.7 CB A:SER29 3.8 15.0 1.0 CA A:SER30 3.9 13.8 1.0 SG A:CYS172 4.0 19.2 1.0 CA A:LEU90 4.0 14.8 0.3 CA A:LEU90 4.0 14.2 0.7 C A:SER89 4.2 14.9 1.0 C A:SER29 4.2 13.8 1.0 CA A:SER29 4.3 14.4 1.0 CA A:SER89 4.4 15.4 1.0 CD2 A:LEU169 4.4 18.4 1.0 S1P A:COA1257 4.5 24.4 1.0 O A:HOH2058 4.7 19.4 1.0 OG A:SER29 4.8 18.6 1.0 NE2 A:HIS228 5.0 17.1 1.0 C A:SER30 5.0 12.9 1.0

Chlorine binding site 2 out of 2 in the Structure of A Thermophilic Esterase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of A Thermophilic Esterase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1256 b:17.8 occ:1.00 OG B:SER30 3.0 17.1 1.0 OG B:SER89 3.0 18.7 1.0 O B:HOH2090 3.1 22.4 1.0 N B:SER30 3.2 14.8 1.0 N B:LEU90 3.2 15.1 1.0 CB B:SER89 3.3 17.0 1.0 CB B:SER30 3.4 16.1 1.0 CB B:LEU90 3.7 17.5 1.0 CA B:SER30 3.9 17.0 1.0 CB B:SER29 3.9 16.5 1.0 SG B:CYS172 3.9 19.4 1.0 CA B:LEU90 4.0 14.6 1.0 C B:SER89 4.2 16.8 1.0 S1P B:COA1255 4.2 19.9 1.0 C B:SER29 4.2 15.2 1.0 CA B:SER29 4.3 15.5 1.0 CA B:SER89 4.3 15.8 1.0 CD2 B:LEU169 4.5 20.3 1.0 O B:HOH2033 4.6 23.0 1.0 OG B:SER29 4.9 18.7 1.0 NE2 B:HIS228 4.9 17.0 1.0

C.Sayer, W.Finnigan, M.N.Isupov, M.Levisson, S.W.Kengen, J.Van Der Oost, N.J.Harmer, J.A.Littlechild. Structural and Biochemical Characterisation of Archaeoglobus Fulgidus Esterase Reveals A Bound Coa Molecule in the Vicinity of the Active Site. Sci.Rep. V. 6 25542 2016.
ISSN: ISSN 2045-2322
PubMed: 27160974
DOI: 10.1038/SREP25542