Magnesium in PDB 6mlf: Crystal Structure of X. Citri Phosphoglucomutase in Complex with 6- Fluoro Glucose 1-Phosphate

Protein crystallography data

The structure of Crystal Structure of X. Citri Phosphoglucomutase in Complex with 6- Fluoro Glucose 1-Phosphate, PDB code: 6mlf was solved by L.Beamer, K.Stiers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.33 / 1.75
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.730, 54.800, 173.550, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / 23.8

Other elements in 6mlf:

The structure of Crystal Structure of X. Citri Phosphoglucomutase in Complex with 6- Fluoro Glucose 1-Phosphate also contains other interesting chemical elements:

Fluorine (F) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of X. Citri Phosphoglucomutase in Complex with 6- Fluoro Glucose 1-Phosphate (pdb code 6mlf). 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 X. Citri Phosphoglucomutase in Complex with 6- Fluoro Glucose 1-Phosphate, PDB code: 6mlf:

Magnesium binding site 1 out of 1 in 6mlf

Go back to Magnesium Binding Sites List in 6mlf
Magnesium binding site 1 out of 1 in the Crystal Structure of X. Citri Phosphoglucomutase in Complex with 6- Fluoro Glucose 1-Phosphate


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 X. Citri Phosphoglucomutase in Complex with 6- Fluoro Glucose 1-Phosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:15.3
occ:1.00
OD2 A:ASP237 1.9 26.3 1.0
O A:HOH660 2.0 27.9 1.0
O2P A:SEP97 2.1 42.3 0.7
OD1 A:ASP239 2.1 25.0 1.0
OD1 A:ASP241 2.1 23.1 1.0
O A:HOH625 2.2 32.4 1.0
CG A:ASP239 2.9 24.0 1.0
CG A:ASP237 3.0 26.1 1.0
P A:SEP97 3.0 50.6 0.7
CG A:ASP241 3.1 29.1 1.0
OD2 A:ASP239 3.1 28.0 1.0
O1P A:SEP97 3.1 35.5 0.7
OD2 A:ASP241 3.4 24.6 1.0
OD1 A:ASP237 3.4 18.8 1.0
O3P A:SEP97 3.5 50.4 0.7
O A:HOH931 4.0 41.3 1.0
O A:HOH604 4.1 24.4 0.3
CB A:ASP237 4.2 16.5 1.0
NE A:ARG242 4.3 31.3 1.0
N A:ASP241 4.3 19.5 1.0
CB A:ASP239 4.4 18.2 1.0
OG A:SEP97 4.4 52.6 0.3
CB A:ASP241 4.4 24.4 1.0
OG A:SEP97 4.5 54.0 0.7
O A:HOH716 4.6 16.2 0.3
N A:ARG242 4.6 15.6 1.0
N A:ASP239 4.7 22.4 1.0
CG A:ARG242 4.7 21.8 1.0
N A:PHE240 4.8 17.7 1.0
CA A:ASP241 4.8 21.1 1.0
NZ A:LYS107 4.8 42.3 1.0
CB A:SEP97 4.8 49.3 0.7
C A:ASP239 4.8 18.8 1.0
CB A:SEP97 4.9 48.3 0.3
CA A:ASP239 4.9 18.8 1.0
C A:ASP241 4.9 20.5 1.0
CD A:ARG242 4.9 25.1 1.0
CA A:SEP97 4.9 42.1 0.7
CA A:SEP97 4.9 43.3 0.3

Reference:

J.S.Zhu, K.M.Stiers, E.Soleimani, B.R.Groves, L.J.Beamer, D.L.Jakeman. Inhibitory Evaluation of Alpha Pmm/Pgm Frompseudomonas Aeruginosa: Chemical Synthesis, Enzyme Kinetics, and Protein Crystallographic Study. J.Org.Chem. V. 84 9627 2019.
ISSN: ISSN 0022-3263
PubMed: 31264865
DOI: 10.1021/ACS.JOC.9B01305
Page generated: Mon Dec 14 23:37:20 2020

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