Magnesium in PDB 6ucw: Multi-Conformer Model of Apo Ketosteroid Isomerase From Pseudomonas Putida (Pksi) at 250 K

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

The structure of Multi-Conformer Model of Apo Ketosteroid Isomerase From Pseudomonas Putida (Pksi) at 250 K, PDB code: 6ucw 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)	36.72 / 1.25
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	35.849, 73.437, 95.989, 90.00, 90.00, 90.00
R / Rfree (%)	14.9 / 17.3

The structure of Multi-Conformer Model of Apo Ketosteroid Isomerase From Pseudomonas Putida (Pksi) 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 Apo Ketosteroid Isomerase From Pseudomonas Putida (Pksi) at 250 K (pdb code 6ucw). 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 Apo Ketosteroid Isomerase From Pseudomonas Putida (Pksi) at 250 K, PDB code: 6ucw:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Multi-Conformer Model of Apo Ketosteroid Isomerase From Pseudomonas Putida (Pksi) 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 Apo Ketosteroid Isomerase From Pseudomonas Putida (Pksi) at 250 K within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg201 b:23.0 occ:0.38 OD2 A:ASP21 1.9 12.2 0.5 O A:HOH380 2.0 23.1 0.8 O A:HOH393 2.1 25.2 0.5 O A:HOH408 2.1 28.5 0.6 O A:HOH385 2.2 31.3 0.6 OD2 A:ASP21 2.4 13.0 0.2 OD2 A:ASP21 2.6 13.0 0.3 CG A:ASP21 3.0 8.5 0.5 HB3 A:ASP21 3.1 8.5 0.5 HB3 A:ASP21 3.2 12.7 0.2 OE1 A:GLU18 3.2 24.9 0.5 HH21 A:ARG67 3.3 22.6 0.5 HB3 A:ASP21 3.4 12.1 0.3 CG A:ASP21 3.5 11.4 0.2 CG A:ASP21 3.5 11.9 0.3 CB A:ASP21 3.6 7.1 0.5 CB A:ASP21 3.8 10.6 0.2 O A:HOH408 3.9 22.8 0.4 HA A:GLU18 3.9 14.2 0.5 CB A:ASP21 4.0 10.1 0.3 NH2 A:ARG67 4.0 18.8 0.5 OD1 A:ASP21 4.0 11.3 0.5 HA A:GLU18 4.0 14.2 0.5 CD A:GLU18 4.0 21.8 0.5 HH22 A:ARG67 4.1 22.6 0.5 HB2 A:ASP21 4.1 8.5 0.5 O A:HOH350 4.1 18.5 1.0 HB2 A:ASP21 4.2 12.7 0.2 OE2 A:GLU18 4.3 25.3 0.5 O A:HOH416 4.3 39.0 1.0 HG2 A:GLU18 4.4 27.2 0.5 HB2 A:ASP21 4.4 12.1 0.3 OD1 A:ASP21 4.5 12.8 0.3 O A:GLU18 4.5 11.9 0.5 HB A:VAL22 4.5 11.3 0.4 HB3 A:GLU18 4.6 17.9 0.5 OD1 A:ASP21 4.6 11.6 0.2 O A:GLU18 4.6 10.6 0.5 HB A:VAL22 4.7 16.8 0.6 C A:ASP21 4.7 9.4 0.5 CA A:ASP21 4.8 8.3 0.5 CA A:GLU18 4.8 11.8 0.5 N A:VAL22 4.8 7.4 0.4 CA A:GLU18 4.9 11.9 0.5 HB3 A:GLU18 4.9 18.2 0.5 H A:VAL22 4.9 8.8 0.5 HE A:ARG67 4.9 19.1 0.5

Magnesium binding site 2 out of 2 in the Multi-Conformer Model of Apo Ketosteroid Isomerase From Pseudomonas Putida (Pksi) 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 Apo Ketosteroid Isomerase From Pseudomonas Putida (Pksi) at 250 K within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg202 b:17.7 occ:0.61 O A:HOH369 2.0 28.2 0.7 O A:HOH405 2.0 27.9 0.7 O A:HOH365 2.0 19.6 0.8 O A:HOH311 2.1 17.6 0.8 O A:HOH321 2.2 22.3 0.6 HE1 A:HIS110 3.8 36.6 0.4 OD2 A:ASP108 3.9 16.2 0.4 OD1 A:ASP35 4.0 11.7 0.3 OD2 A:ASP35 4.0 14.5 0.3 O A:HOH326 4.2 23.1 1.0 OE1 A:GLN114 4.2 16.8 0.6 HB1 A:ALA33 4.3 13.9 0.5 HB1 A:ALA33 4.3 10.2 0.5 ND1 A:HIS110 4.3 30.7 0.4 OD1 A:ASP35 4.4 16.4 0.7 CG A:ASP35 4.4 12.7 0.3 CE1 A:HIS110 4.4 30.5 0.4 OD2 A:ASP108 4.4 16.0 0.6 OE1 A:GLN114 4.4 22.8 0.4 OD2 A:ASP34 4.5 16.8 0.6 HD2 A:HIS110 4.6 30.4 0.6 HE22 A:GLN114 4.7 20.5 0.6 OD2 A:ASP34 4.7 11.3 0.4 OE2 A:GLU109 4.7 47.5 0.5 OD2 A:ASP35 4.7 21.0 0.7 HB2 A:ASP108 4.8 15.4 0.4 HE22 A:GLN114 4.8 28.0 0.4 CG A:ASP108 4.8 15.3 0.4 CG A:ASP35 4.9 17.6 0.7 HB2 A:ASP108 4.9 14.7 0.6

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