Chlorine in PDB 6ucn: Multi-Conformer Model of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) Bound to Equilenin at 250 K

All present enzymatic activity of Multi-Conformer Model of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) Bound to Equilenin at 250 K:
5.3.3.1;

The structure of Multi-Conformer Model of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) Bound to Equilenin at 250 K, PDB code: 6ucn was solved by F.Yabukarski, D.Herschlag, J.T.Biel, J.S.Fraser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.29 / 1.32
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	35.907, 73.724, 95.727, 90.00, 90.00, 90.00
R / Rfree (%)	14.4 / 17.4

The structure of Multi-Conformer Model of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) Bound to Equilenin at 250 K also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Chlorine atom in the Multi-Conformer Model of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) Bound to Equilenin at 250 K (pdb code 6ucn). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Multi-Conformer Model of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) Bound to Equilenin at 250 K, PDB code: 6ucn:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Multi-Conformer Model of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) Bound to Equilenin at 250 K


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Multi-Conformer Model of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) Bound to Equilenin at 250 K within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:19.2 occ:0.75 HH22 A:ARG75 2.1 14.3 0.1 HH12 A:ARG75 2.2 12.8 0.8 HG1 B:THR71 2.5 13.6 0.2 HH22 A:ARG75 2.5 12.5 0.8 HA3 A:GLY72 2.6 15.7 0.3 HA3 A:GLY72 2.7 15.5 0.4 O B:HOH426 2.7 19.2 0.3 HG1 B:THR71 2.7 17.1 0.5 HA3 A:GLY72 2.8 12.4 0.3 O B:HOH389 2.8 25.4 1.0 HD2 A:PRO73 2.9 16.2 0.7 OG1 B:THR71 2.9 14.2 0.5 NH2 A:ARG75 2.9 11.9 0.1 O B:HOH328 2.9 20.6 0.4 HH12 A:ARG75 3.0 10.1 0.1 HG1 B:THR71 3.0 13.3 0.3 NH1 A:ARG75 3.0 10.6 0.8 HB2 B:PRO85 3.1 12.7 0.5 OG1 B:THR71 3.2 11.3 0.2 NH2 A:ARG75 3.2 10.4 0.8 HB2 B:PRO85 3.2 11.4 0.5 HB B:THR71 3.4 15.0 0.2 OG1 B:THR71 3.4 11.1 0.3 HG3 A:PRO85 3.4 13.2 0.7 HB B:THR71 3.4 15.1 0.5 HG21 B:THR71 3.4 13.6 0.2 HH21 A:ARG75 3.5 14.3 0.1 HD2 A:PRO73 3.5 19.1 0.3 O B:HOH328 3.5 26.6 0.6 O B:HOH426 3.5 38.7 0.7 HG3 A:PRO85 3.5 10.3 0.3 CZ A:ARG75 3.6 11.5 0.8 CA A:GLY72 3.6 13.1 0.3 CA A:GLY72 3.6 12.9 0.4 NH1 A:ARG75 3.6 8.4 0.1 CB B:THR71 3.7 12.6 0.5 CB B:THR71 3.7 12.5 0.2 HH11 A:ARG75 3.7 12.8 0.8 CZ A:ARG75 3.7 11.5 0.1 HB B:THR71 3.7 12.9 0.3 HA2 A:GLY72 3.7 15.5 0.4 CA A:GLY72 3.7 10.3 0.3 CD A:PRO73 3.8 13.5 0.7 HA2 A:GLY72 3.8 15.7 0.3 HH21 A:ARG75 3.9 12.5 0.8 CB B:PRO85 4.0 10.5 0.5 HA2 A:GLY72 4.0 12.4 0.3 HG2 A:PRO85 4.0 13.2 0.7 CG2 B:THR71 4.1 11.3 0.2 CB B:PRO85 4.1 9.5 0.5 HG21 B:THR71 4.1 14.4 0.5 CB B:THR71 4.1 10.7 0.3 O A:THR71 4.1 14.7 0.5 CG A:PRO85 4.1 10.9 0.7 CD A:PRO73 4.2 15.9 0.3 HD3 A:PRO73 4.2 19.1 0.3 HB3 B:PRO85 4.2 11.4 0.5 HD3 A:PRO73 4.2 16.2 0.7 HB3 B:PRO85 4.2 12.7 0.5 HG2 A:PRO85 4.2 10.3 0.3 O B:THR71 4.2 13.3 0.3 C A:GLY72 4.3 11.8 0.3 CG A:PRO85 4.3 8.6 0.3 N A:PRO73 4.3 12.8 0.7 C A:GLY72 4.4 11.1 0.4 HH11 A:ARG75 4.4 10.1 0.1 HG2 B:PRO85 4.5 10.4 0.5 CG2 B:THR71 4.5 12.0 0.5 N A:GLY72 4.5 12.8 0.3 O A:THR71 4.5 14.5 0.3 N A:GLY72 4.5 11.8 0.3 N A:GLY72 4.5 13.0 0.4 HG2 A:PRO73 4.5 20.1 0.7 C A:GLY72 4.5 12.8 0.3 N A:PRO73 4.6 9.5 0.3 O A:THR71 4.6 14.4 0.3 HG23 B:THR71 4.7 13.6 0.2 CG B:PRO85 4.7 8.7 0.5 HG22 B:THR71 4.7 13.6 0.2 C A:THR71 4.7 13.0 0.5 CG A:PRO73 4.8 16.8 0.7 HG3 B:PRO85 4.8 10.4 0.5 C B:THR71 4.8 9.7 0.3 HB3 B:ASP100 4.8 13.7 0.7 O B:THR71 4.8 13.2 0.5 C A:THR71 4.8 14.3 0.3 C A:THR71 4.9 13.1 0.3 NE A:ARG75 4.9 10.0 0.8 HG2 B:PRO85 4.9 11.4 0.5 HG21 B:THR71 4.9 13.6 0.3 CA B:THR71 4.9 10.0 0.5 C B:THR71 5.0 12.8 0.5 CG B:PRO85 5.0 9.5 0.5 NE A:ARG75 5.0 9.8 0.1

Chlorine binding site 2 out of 2 in the Multi-Conformer Model of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) Bound to Equilenin at 250 K


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Multi-Conformer Model of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) Bound to Equilenin at 250 K within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl204 b:20.0 occ:0.77 HH22 B:ARG75 2.2 11.9 0.2 HH12 B:ARG75 2.2 13.0 0.5 HG1 A:THR71 2.2 16.4 0.3 HH22 B:ARG75 2.4 12.5 0.5 HH12 B:ARG75 2.4 10.9 0.2 HH12 B:ARG75 2.5 11.8 0.3 HG1 A:THR71 2.5 16.9 0.3 HA3 B:GLY72 2.6 14.6 0.7 HH22 B:ARG75 2.7 10.4 0.3 HG1 A:THR71 2.7 17.5 0.5 O A:HOH342 2.8 22.3 0.4 HD2 B:PRO73 2.8 14.6 0.7 O B:HOH389 2.8 25.4 1.0 HA3 B:GLY72 2.9 17.5 0.3 NH2 B:ARG75 2.9 9.9 0.2 OG1 A:THR71 3.0 13.6 0.3 NH1 B:ARG75 3.0 10.8 0.5 OG1 A:THR71 3.1 14.1 0.3 NH1 B:ARG75 3.1 9.1 0.2 NH2 B:ARG75 3.1 10.4 0.5 OG1 A:THR71 3.1 14.6 0.5 HB2 A:PRO85 3.2 11.6 0.7 O A:HOH342 3.2 28.4 0.6 NH1 B:ARG75 3.3 9.8 0.3 HB2 A:PRO85 3.3 14.2 0.3 HB A:THR71 3.4 16.4 0.3 HG3 B:PRO85 3.4 11.4 0.5 NH2 B:ARG75 3.4 8.7 0.3 CZ B:ARG75 3.5 7.0 0.2 HB A:THR71 3.5 15.6 0.3 HB A:THR71 3.5 17.1 0.5 CZ B:ARG75 3.5 9.5 0.5 HG3 B:PRO85 3.5 10.4 0.5 CA B:GLY72 3.5 12.1 0.7 HH21 B:ARG75 3.6 11.9 0.2 HG21 A:THR71 3.6 21.4 0.3 HD2 B:PRO73 3.7 13.0 0.3 HH11 B:ARG75 3.7 13.0 0.5 CB A:THR71 3.7 12.9 0.3 HA2 B:GLY72 3.7 14.6 0.7 CD B:PRO73 3.7 12.2 0.7 CB A:THR71 3.7 13.6 0.3 CZ B:ARG75 3.8 7.2 0.3 CA B:GLY72 3.9 14.5 0.3 CB A:THR71 3.9 14.2 0.5 HH11 B:ARG75 3.9 10.9 0.2 HH21 B:ARG75 3.9 12.5 0.5 HH11 B:ARG75 4.0 11.8 0.3 HG2 B:PRO85 4.0 10.4 0.5 CB A:PRO85 4.0 9.6 0.7 O B:THR71 4.0 13.3 0.3 HB3 A:PRO85 4.1 11.6 0.7 HD3 B:PRO73 4.1 14.6 0.7 HH21 B:ARG75 4.1 10.4 0.3 HG21 A:THR71 4.2 22.1 0.3 CG2 A:THR71 4.2 17.8 0.3 HA2 B:GLY72 4.2 17.5 0.3 CB A:PRO85 4.2 11.8 0.3 HG2 B:PRO85 4.2 11.4 0.5 CG B:PRO85 4.2 8.7 0.5 CG B:PRO85 4.2 9.5 0.5 N B:PRO73 4.3 11.3 0.7 C B:GLY72 4.3 10.9 0.7 O A:THR71 4.3 14.7 0.5 CD B:PRO73 4.3 10.8 0.3 HD3 B:PRO73 4.4 13.0 0.3 O B:THR71 4.4 13.2 0.5 HG2 B:PRO73 4.5 15.7 0.7 HG2 A:PRO85 4.5 10.3 0.3 HB3 A:PRO85 4.5 14.2 0.3 N B:GLY72 4.5 11.2 0.7 CG2 A:THR71 4.5 18.4 0.3 HG21 A:THR71 4.6 17.6 0.5 N B:GLY72 4.6 11.6 0.3 C B:GLY72 4.7 13.4 0.3 C B:THR71 4.7 9.7 0.3 HG23 A:THR71 4.7 21.4 0.3 CG B:PRO73 4.7 13.0 0.7 CG A:PRO85 4.7 8.6 0.3 HG3 A:PRO85 4.7 10.3 0.3 N B:PRO73 4.7 9.3 0.3 O B:THR71 4.7 12.2 0.2 HB3 A:ASP100 4.8 11.1 0.3 NE B:ARG75 4.8 9.0 0.2 C B:THR71 4.8 12.8 0.5 HG2 A:PRO85 4.8 13.2 0.7 O A:THR71 4.8 14.5 0.3 C A:THR71 4.8 13.0 0.5 NE B:ARG75 4.8 10.0 0.5 CG2 A:THR71 4.8 14.6 0.5 H A:PHE86 4.9 10.2 0.3 O A:HOH345 4.9 51.5 1.0 CG A:PRO85 4.9 10.9 0.7 HG22 A:THR71 4.9 21.4 0.3 O B:HOH433 4.9 33.9 0.6 C B:THR71 4.9 12.2 0.2 C A:THR71 4.9 13.1 0.3 CA A:THR71 5.0 14.5 0.5 HB2 B:PRO85 5.0 11.4 0.5 CA A:THR71 5.0 14.4 0.3 HB3 B:PRO85 5.0 11.4 0.5 HG3 A:PRO85 5.0 13.2 0.7 CB B:PRO85 5.0 9.5 0.5

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