Atomistry » Magnesium » PDB 6mlq-6mxc » 6mnv
Atomistry »
  Magnesium »
    PDB 6mlq-6mxc »
      6mnv »

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

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy