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Magnesium in PDB 6u4i: Crystal Structure of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) Bound to Equilenin at 280 K

Enzymatic activity of Crystal Structure of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) Bound to Equilenin at 280 K

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

Protein crystallography data

The structure of Crystal Structure of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) Bound to Equilenin at 280 K, PDB code: 6u4i 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) 36.83 / 1.55
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 35.542, 73.663, 95.683, 90.00, 90.00, 90.00
R / Rfree (%) 13.7 / 17.5

Other elements in 6u4i:

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

Chlorine (Cl) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) Bound to Equilenin at 280 K (pdb code 6u4i). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) Bound to Equilenin at 280 K, PDB code: 6u4i:

Magnesium binding site 1 out of 1 in 6u4i

Go back to Magnesium Binding Sites List in 6u4i
Magnesium binding site 1 out of 1 in the Crystal Structure of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) Bound to Equilenin at 280 K


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Ketosteroid Isomerase From Pseudomonas Putida (Pksi) Bound to Equilenin at 280 K within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg202

b:38.3
occ:0.70
 O B:HOH382 2.0 39.3 0.7
O B:HOH303 2.1 31.9 0.8
O B:HOH325 2.1 25.4 0.8
O B:HOH341 2.2 35.3 0.7
O B:HOH313 4.0 31.1 1.0
OE1 B:GLN114 4.1 22.4 0.7
OD1 B:ASP35 4.1 21.6 1.0
OD2 B:ASP108 4.3 22.3 1.0
HB1 B:ALA33 4.3 16.2 1.0
OD2 B:ASP35 4.4 24.3 1.0
HD2 B:HIS110 4.4 44.0 1.0
HE22 B:GLN114 4.5 26.2 0.7
CG B:ASP35 4.6 22.1 1.0
OD2 B:ASP34 4.6 25.1 1.0
OE1 B:GLU109 4.9 39.4 0.6
HB2 B:ASP108 4.9 22.7 1.0

Reference:

F.Yabukarski, D.Herschlag. Assessing Active Site Positioning and Testing Catalytic Proposals Via Ketosteroid Isomerase Conformational Ensembles To Be Published.
Page generated: Tue Oct 1 20:50:21 2024

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