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Magnesium in PDB 6mnv: Crystal Structure of X. Citri Phosphoglucomutase in Complex with CH2FG1P

Enzymatic activity of Crystal Structure of X. Citri Phosphoglucomutase in Complex with CH2FG1P

All present enzymatic activity of Crystal Structure of X. Citri Phosphoglucomutase in Complex with CH2FG1P:
5.4.2.2;

Protein crystallography data

The structure of Crystal Structure of X. Citri Phosphoglucomutase in Complex with CH2FG1P, PDB code: 6mnv 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) 42.30 / 1.65
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.650, 54.460, 171.160, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 20.4

Other elements in 6mnv:

The structure of Crystal Structure of X. Citri Phosphoglucomutase in Complex with CH2FG1P 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 CH2FG1P (pdb code 6mnv). 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 CH2FG1P, PDB code: 6mnv:

Magnesium binding site 1 out of 1 in 6mnv

Go back to Magnesium Binding Sites List in 6mnv
Magnesium binding site 1 out of 1 in the Crystal Structure of X. Citri Phosphoglucomutase in Complex with CH2FG1P


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 CH2FG1P within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:15.8
occ:1.00
 OD2 A:ASP237 1.9 20.8 1.0
OD1 A:ASP239 2.1 22.3 1.0
OD1 A:ASP241 2.1 20.2 1.0
O A:HOH833 2.1 24.8 1.0
O A:HOH638 2.1 22.0 1.0
OG A:SER97 2.3 26.4 1.0
CG A:ASP237 3.0 19.9 1.0
CG A:ASP239 3.0 22.1 1.0
CG A:ASP241 3.0 26.4 1.0
OD2 A:ASP239 3.2 21.2 1.0
OD2 A:ASP241 3.4 25.7 1.0
CB A:SER97 3.4 34.8 1.0
OD1 A:ASP237 3.4 16.7 1.0
O A:HOH854 4.0 47.4 1.0
CA A:SER97 4.1 33.4 1.0
O A:HOH850 4.1 39.0 1.0
CB A:ASP237 4.2 15.3 1.0
NE A:ARG242 4.2 24.7 1.0
N A:ASP241 4.3 17.3 1.0
CB A:ASP241 4.4 16.8 1.0
CB A:ASP239 4.4 19.0 1.0
ND1 A:HIS98 4.6 37.3 1.0
N A:ARG242 4.7 14.8 1.0
NH2 A:ARG242 4.7 23.1 1.0
N A:ASP239 4.7 16.9 1.0
C A:SER97 4.7 39.5 1.0
CA A:ASP241 4.8 16.1 1.0
C A:ASP239 4.9 19.3 1.0
CA A:ASP239 4.9 20.6 1.0
CG A:ARG242 4.9 17.9 1.0
N A:PHE240 4.9 19.5 1.0
C A:ASP241 4.9 17.0 1.0
CZ A:ARG242 5.0 25.0 1.0

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: Tue Oct 1 11:55:29 2024

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