Magnesium 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:

Chlorine

(Cl)

2 atoms

The binding sites of Magnesium 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 Magnesium atom.
In total 2 binding sites of Magnesium 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 Magnesium binding site number: 1; 2;

Magnesium 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 Magnesium with other atoms in the Mg 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 B:Mg202 b:18.8 occ:0.47 O B:HOH410 2.0 33.6 0.8 O B:HOH396 2.0 32.8 0.7 O B:HOH360 2.1 20.6 0.8 O B:HOH304 2.1 21.1 0.6 O B:HOH351 2.3 28.3 0.7 OD2 B:ASP108 3.9 15.7 0.2 OD2 B:ASP108 4.0 12.2 0.4 O B:HOH316 4.0 23.6 1.0 HB1 B:ALA33 4.1 13.5 0.3 OD1 B:ASP35 4.1 15.4 0.7 OE1 B:GLN114 4.2 23.7 0.8 HD2 B:HIS110 4.3 23.2 0.3 OD2 B:ASP35 4.3 24.1 0.7 HB1 B:ALA33 4.4 15.1 0.7 OD2 B:ASP108 4.4 14.7 0.5 O B:HOH408 4.5 38.3 0.4 OD2 B:ASP34 4.6 19.2 0.7 CG B:ASP35 4.6 17.9 0.7 HB2 B:ASP108 4.6 15.8 0.2 HE1 B:HIS110 4.7 32.5 0.4 HE22 B:GLN114 4.7 25.6 0.8 ND1 B:HIS110 4.8 31.1 0.4 O B:ASP34 4.8 14.3 0.3 HB2 B:ASP108 4.9 15.5 0.4 CG B:ASP108 4.9 11.4 0.4 HB3 B:ASP34 4.9 14.2 0.3 CG B:ASP108 4.9 11.9 0.2 HB2 B:ASP108 4.9 14.0 0.5 CB B:ALA33 5.0 11.3 0.3 HE2 B:HIS110 5.0 32.0 0.3

Magnesium 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 Magnesium with other atoms in the Mg 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:Mg203 b:31.6 occ:0.55 OD2 B:ASP21 1.8 17.2 0.3 O B:HOH413 1.9 25.7 0.6 O B:HOH329 2.0 22.1 0.7 OD2 B:ASP21 2.5 14.7 0.5 O B:HOH343 2.5 33.4 0.5 O B:HOH371 2.7 37.3 0.6 OD2 B:ASP21 2.8 11.9 0.1 HB3 B:ASP21 2.9 12.2 0.3 CG B:ASP21 2.9 17.4 0.3 OE1 B:GLU18 3.0 26.3 0.4 HB3 B:ASP21 3.1 12.9 0.1 O B:HOH343 3.2 32.3 0.5 HB3 B:ASP21 3.3 12.9 0.5 CB B:ASP21 3.4 10.2 0.3 CG B:ASP21 3.5 14.3 0.1 CG B:ASP21 3.5 12.0 0.5 HH21 B:ARG67 3.7 24.0 0.3 HG2 B:GLU18 3.7 21.4 0.3 HA B:GLU18 3.8 11.2 0.4 CB B:ASP21 3.8 10.8 0.1 HH22 B:ARG67 3.8 24.9 0.3 HB2 B:ASP21 3.9 12.2 0.3 CB B:ASP21 3.9 10.7 0.5 CD B:GLU18 3.9 21.8 0.4 HA B:GLU18 3.9 13.8 0.3 OD1 B:ASP21 4.0 11.5 0.3 HA B:GLU18 4.0 12.5 0.3 O B:HOH307 4.1 20.5 1.0 HB3 B:GLU18 4.1 13.8 0.4 O B:HOH371 4.2 24.9 0.4 HB2 B:ASP21 4.2 12.9 0.1 O B:GLU18 4.3 9.8 0.3 O B:HOH428 4.3 45.5 1.0 HB B:VAL22 4.3 12.5 0.2 HB2 B:ASP21 4.3 12.9 0.5 NH2 B:ARG67 4.3 20.8 0.3 NH2 B:ARG67 4.4 20.0 0.3 HH12 B:ARG67 4.4 27.2 0.3 OE2 B:GLU18 4.4 25.7 0.4 OD1 B:ASP21 4.5 15.6 0.1 HG2 B:GLU18 4.5 17.6 0.3 HB B:VAL22 4.5 13.5 0.4 C B:ASP21 4.5 9.5 0.3 O B:GLU18 4.5 10.3 0.3 O B:GLU18 4.6 8.8 0.4 CA B:GLU18 4.6 9.3 0.4 CA B:ASP21 4.6 9.1 0.3 HH22 B:ARG67 4.6 24.0 0.3 CG B:GLU18 4.6 17.8 0.3 OD1 B:ASP21 4.6 13.3 0.5 N B:VAL22 4.7 9.5 0.4 HH21 B:ARG67 4.7 24.9 0.3 HB B:VAL22 4.7 11.9 0.4 CB B:GLU18 4.7 11.5 0.4 H B:VAL22 4.7 11.5 0.3 CA B:GLU18 4.8 11.5 0.3 HG3 B:GLU18 4.8 21.4 0.3 O B:ASP21 4.9 10.1 0.3 NH1 B:ARG67 4.9 22.7 0.3 CA B:GLU18 4.9 10.4 0.3 HB3 B:GLU18 4.9 16.1 0.3 CZ B:ARG67 4.9 22.4 0.3 H B:VAL22 4.9 9.6 0.5 CG B:GLU18 4.9 15.2 0.4 HA B:VAL22 5.0 12.2 0.4 C B:GLU18 5.0 8.8 0.3

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