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Magnesium in PDB 6c17: Crystal Structure of Ketosteroid Isomerase D40N Mutant From Pseudomonas Putida (Pksi) Bound to 3,4-Dinitrophenol

Enzymatic activity of Crystal Structure of Ketosteroid Isomerase D40N Mutant From Pseudomonas Putida (Pksi) Bound to 3,4-Dinitrophenol

All present enzymatic activity of Crystal Structure of Ketosteroid Isomerase D40N Mutant From Pseudomonas Putida (Pksi) Bound to 3,4-Dinitrophenol:
5.3.3.1;

Protein crystallography data

The structure of Crystal Structure of Ketosteroid Isomerase D40N Mutant From Pseudomonas Putida (Pksi) Bound to 3,4-Dinitrophenol, PDB code: 6c17 was solved by F.Yabukarski, M.Pinney, D.Herschlag, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.42 / 1.10
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 35.881, 94.763, 72.847, 90.00, 90.00, 90.00
R / Rfree (%) 14.7 / 17.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Ketosteroid Isomerase D40N Mutant From Pseudomonas Putida (Pksi) Bound to 3,4-Dinitrophenol (pdb code 6c17). 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 D40N Mutant From Pseudomonas Putida (Pksi) Bound to 3,4-Dinitrophenol, PDB code: 6c17:

Magnesium binding site 1 out of 1 in 6c17

Go back to Magnesium Binding Sites List in 6c17
Magnesium binding site 1 out of 1 in the Crystal Structure of Ketosteroid Isomerase D40N Mutant From Pseudomonas Putida (Pksi) Bound to 3,4-Dinitrophenol


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 D40N Mutant From Pseudomonas Putida (Pksi) Bound to 3,4-Dinitrophenol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg201

b:22.3
occ:0.60
 O A:HOH351 2.0 23.7 0.7
O A:HOH421 2.0 30.8 0.6
O A:HOH308 2.0 21.3 0.7
O A:HOH396 2.1 25.4 0.6
O A:HOH371 2.1 23.8 0.6
HB1 A:ALA33 4.1 15.2 1.0
OD1 A:ASP35 4.2 20.8 1.0
HE1 A:HIS110 4.2 40.2 1.0
OD2 A:ASP108 4.2 21.7 1.0
OE1 A:GLN114 4.2 19.7 0.7
O A:HOH303 4.3 25.2 1.0
OD2 A:ASP34 4.5 21.8 1.0
OD2 A:ASP35 4.5 25.9 1.0
O A:HOH355 4.5 35.8 1.0
O A:HOH352 4.7 21.5 1.0
HE21 A:GLN114 4.7 26.1 0.3
CG A:ASP35 4.7 21.0 1.0
HE22 A:GLN114 4.7 20.9 0.7
OE1 A:GLU109 4.8 31.4 0.5
CE1 A:HIS110 4.9 33.5 1.0
ND1 A:HIS110 4.9 31.2 1.0
HB2 A:ASP108 4.9 20.8 1.0

Reference:

M.M.Pinney, A.Natarajan, F.Yabukarski, D.M.Sanchez, F.Liu, R.Liang, T.Doukov, J.P.Schwans, T.J.Martinez, D.Herschlag. Structural Coupling Throughout the Active Site Hydrogen Bond Networks of Ketosteroid Isomerase and Photoactive Yellow Protein. J. Am. Chem. Soc. V. 140 9827 2018.
ISSN: ESSN 1520-5126
PubMed: 29990421
DOI: 10.1021/JACS.8B01596
Page generated: Mon Sep 30 20:05:53 2024

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