Chlorine in PDB 4qlx: Crystal Structure of Cla-Er with Product Binding

The structure of Crystal Structure of Cla-Er with Product Binding, PDB code: 4qlx was solved by F.Hou, T.Miyakawa, M.Tanokura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.90 / 1.95
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	64.933, 68.850, 197.497, 90.00, 90.00, 90.00
R / Rfree (%)	18.7 / 23

The binding sites of Chlorine atom in the Crystal Structure of Cla-Er with Product Binding (pdb code 4qlx). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 5 binding sites of Chlorine where determined in the Crystal Structure of Cla-Er with Product Binding, PDB code: 4qlx:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5;

Chlorine binding site 1 out of 5 in the Crystal Structure of Cla-Er with Product Binding


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 Cla-Er with Product Binding within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl303 b:54.8 occ:1.00 SD A:MET1 3.5 71.3 1.0 CB A:SER2 3.5 39.5 1.0 CG A:MET1 3.5 51.6 1.0 N A:SER2 3.7 40.6 1.0 N A:GLU3 3.9 45.7 1.0 CA A:SER2 4.0 41.0 1.0 CE A:MET1 4.1 51.0 1.0 OE2 A:GLU3 4.2 48.0 1.0 CD A:GLU3 4.3 48.1 1.0 C A:SER2 4.5 43.4 1.0 CG A:GLU3 4.5 36.3 1.0 CB A:GLU3 4.6 39.7 1.0 OE1 A:GLU3 4.7 46.2 1.0 C A:MET1 4.8 43.6 1.0 CB A:MET1 4.8 48.6 1.0 CA A:GLU3 4.9 44.3 1.0

Chlorine binding site 2 out of 5 in the Crystal Structure of Cla-Er with Product Binding


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Cla-Er with Product Binding within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl304 b:48.8 occ:1.00 O A:HOH530 3.4 31.8 1.0 O A:HOH502 3.5 25.8 1.0 CA A:GLY33 3.5 29.6 1.0 N A:GLU36 3.6 22.5 1.0 C A:GLY33 3.9 28.2 1.0 CB A:ASP35 3.9 26.3 1.0 CB A:GLU36 3.9 23.7 1.0 N A:GLY33 4.1 29.1 1.0 O A:GLY33 4.1 26.0 1.0 N A:ASP35 4.2 23.5 1.0 CA A:GLU36 4.3 23.8 1.0 C A:ASP35 4.4 28.2 1.0 CA A:ASP35 4.4 28.0 1.0 O A:HOH532 4.6 39.0 1.0 N A:ARG34 4.7 30.0 1.0 CG A:ASP35 4.8 37.8 1.0 OD2 A:ASP35 4.8 44.0 1.0

Chlorine binding site 3 out of 5 in the Crystal Structure of Cla-Er with Product Binding


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Cla-Er with Product Binding within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl305 b:46.8 occ:1.00 O A:HOH476 3.4 27.1 1.0 N A:LYS76 3.7 27.3 1.0 CG A:LYS76 3.8 29.5 1.0 CA A:MET75 4.0 28.5 1.0 CB A:MET75 4.1 24.3 1.0 CG A:MET75 4.4 30.2 1.0 C A:MET75 4.4 26.5 1.0 CB A:LYS76 4.5 28.8 1.0 NZ A:LYS76 4.7 49.1 1.0 CA A:LYS76 4.7 25.2 1.0 CE A:MET75 4.9 30.6 1.0

Chlorine binding site 4 out of 5 in the Crystal Structure of Cla-Er with Product Binding


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of Cla-Er with Product Binding within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl306 b:56.7 occ:1.00 NH1 A:ARG102 3.6 39.7 1.0 NH2 A:ARG102 3.9 48.0 1.0 CZ A:ARG102 4.2 43.3 1.0 CB A:LEU123 4.7 27.9 1.0

Chlorine binding site 5 out of 5 in the Crystal Structure of Cla-Er with Product Binding


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Crystal Structure of Cla-Er with Product Binding within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl303 b:40.1 occ:1.00 O B:HOH407 3.4 24.2 1.0 N B:LYS76 3.7 23.5 1.0 CA B:MET75 3.9 21.9 1.0 CG B:LYS76 4.1 29.8 1.0 CB B:MET75 4.1 22.6 1.0 CE B:LYS76 4.3 43.6 1.0 C B:MET75 4.3 22.0 1.0 CG B:MET75 4.5 25.0 1.0 CB B:LYS76 4.5 26.4 1.0 CE B:MET75 4.5 21.0 1.0 CD B:LYS76 4.6 40.4 1.0 CA B:LYS76 4.7 22.2 1.0

F.Hou, T.Miyakawa, N.Kitamura, M.Takeuchi, S.Park, S.Kishino, J.Ogawa, M.Tanokura. Structure and Reaction Mechanism of A Novel Enone Reductase Catalyzing A Key Step of A Gut-Bacterial Fatty Acid Saturation Metabolism, Biohydrogenation To Be Published.