Chlorine in PDB 6u1z: Crystal Structure of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) at 280 K

All present enzymatic activity of Crystal Structure of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) at 280 K:
5.3.3.1;

The structure of Crystal Structure of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) at 280 K, PDB code: 6u1z was solved by F.Yabukarski, D.Herschlag, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.97 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	36.028, 73.938, 95.691, 90.00, 90.00, 90.00
R / Rfree (%)	13.6 / 16.7

The structure of Crystal Structure of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) at 280 K also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Chlorine atom in the Crystal Structure of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) at 280 K (pdb code 6u1z). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) at 280 K, PDB code: 6u1z:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) at 280 K


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 Ketosteroid Isomerase From Pseudomonas Putida (Pksi) at 280 K within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl202 b:28.1 occ:0.84 HH12 B:ARG75 2.3 20.1 1.0 HH22 B:ARG75 2.4 20.6 1.0 HG1 A:THR71 2.6 29.3 1.0 HA3 B:GLY72 2.7 22.1 1.0 O B:HOH378 2.8 31.7 1.0 HD2 B:PRO73 3.0 24.6 1.0 HB2 A:PRO85 3.1 20.4 1.0 NH1 B:ARG75 3.1 16.7 1.0 OG1 A:THR71 3.1 24.4 1.0 NH2 B:ARG75 3.2 17.1 1.0 HG3 B:PRO85 3.4 20.3 1.0 HB A:THR71 3.5 27.5 1.0 CZ B:ARG75 3.6 14.6 1.0 CA B:GLY72 3.7 18.4 1.0 HH11 B:ARG75 3.8 20.1 1.0 CB A:THR71 3.9 22.9 1.0 CD B:PRO73 3.9 20.5 1.0 HH21 B:ARG75 3.9 20.6 1.0 HA2 B:GLY72 3.9 22.1 1.0 CB A:PRO85 3.9 17.0 1.0 HB3 A:PRO85 4.1 20.4 1.0 HG2 B:PRO85 4.1 20.3 1.0 CG B:PRO85 4.2 16.9 1.0 HD3 B:PRO73 4.3 24.6 1.0 O B:THR71 4.3 22.7 1.0 C B:GLY72 4.4 17.1 1.0 HG21 A:THR71 4.4 30.5 1.0 N B:PRO73 4.4 18.3 1.0 N B:GLY72 4.5 18.2 1.0 HG2 B:PRO73 4.6 26.3 1.0 HG2 A:PRO85 4.6 22.7 1.0 O A:THR71 4.7 25.2 1.0 CG A:PRO85 4.8 18.9 1.0 CG2 A:THR71 4.8 25.4 1.0 C B:THR71 4.8 19.0 1.0 HG3 A:PRO85 4.8 22.7 1.0 CG B:PRO73 4.8 21.9 1.0 NE B:ARG75 4.9 15.5 1.0 HB3 A:ASP100 4.9 21.0 1.0 C A:THR71 5.0 21.4 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) at 280 K


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 Ketosteroid Isomerase From Pseudomonas Putida (Pksi) at 280 K within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:25.7 occ:0.77 HH12 A:ARG75 2.3 21.5 1.0 HH22 A:ARG75 2.4 21.4 1.0 HG1 B:THR71 2.6 28.7 1.0 HA3 A:GLY72 2.7 21.8 1.0 O B:HOH378 2.8 31.7 1.0 HD2 A:PRO73 2.9 26.2 1.0 O B:HOH355 2.9 50.2 1.0 NH1 A:ARG75 3.1 17.9 1.0 OG1 B:THR71 3.1 23.9 1.0 HB2 B:PRO85 3.1 18.9 1.0 NH2 A:ARG75 3.2 17.9 1.0 HG3 A:PRO85 3.4 22.7 1.0 HB B:THR71 3.5 26.2 1.0 CZ A:ARG75 3.6 14.6 1.0 CA A:GLY72 3.7 18.1 1.0 HH11 A:ARG75 3.8 21.5 1.0 CB B:THR71 3.8 21.8 1.0 CD A:PRO73 3.9 21.8 1.0 HH21 A:ARG75 3.9 21.4 1.0 HA2 A:GLY72 3.9 21.8 1.0 CB B:PRO85 4.0 15.7 1.0 HG2 A:PRO85 4.1 22.7 1.0 HB3 B:PRO85 4.1 18.9 1.0 CG A:PRO85 4.2 18.9 1.0 HG21 B:THR71 4.3 27.6 1.0 O A:THR71 4.3 25.2 1.0 HD3 A:PRO73 4.3 26.2 1.0 N A:PRO73 4.4 19.6 1.0 C A:GLY72 4.4 18.0 1.0 HG2 A:PRO73 4.5 30.4 1.0 N A:GLY72 4.6 20.9 1.0 HG2 B:PRO85 4.6 20.3 1.0 CG2 B:THR71 4.7 22.9 1.0 O B:THR71 4.7 22.7 1.0 CG A:PRO73 4.8 25.3 1.0 C A:THR71 4.8 21.4 1.0 CG B:PRO85 4.8 16.9 1.0 HG3 B:PRO85 4.9 20.3 1.0 NE A:ARG75 4.9 15.5 1.0 HB3 B:ASP100 4.9 25.4 1.0 C B:THR71 5.0 19.0 1.0

F.Yabukarski, D.Herschlag. Assessing Active Site Positioning and Testing Catalytic Proposals Via Ketosteroid Isomerase Conformational Ensembles To Be Published.