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Magnesium in PDB 5bmp: Crystal Structure of Phosphoglucomutase From Xanthomonas Citri Complexed with Glucose-1-Phosphate

Enzymatic activity of Crystal Structure of Phosphoglucomutase From Xanthomonas Citri Complexed with Glucose-1-Phosphate

All present enzymatic activity of Crystal Structure of Phosphoglucomutase From Xanthomonas Citri Complexed with Glucose-1-Phosphate:
5.4.2.2;

Protein crystallography data

The structure of Crystal Structure of Phosphoglucomutase From Xanthomonas Citri Complexed with Glucose-1-Phosphate, PDB code: 5bmp was solved by L.S.Goto, H.M.Pereira, M.T.M.Novo Mansur, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.56 / 1.85
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.861, 54.732, 173.143, 90.00, 90.00, 90.00
R / Rfree (%) 15.2 / 18

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Phosphoglucomutase From Xanthomonas Citri Complexed with Glucose-1-Phosphate (pdb code 5bmp). 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 Phosphoglucomutase From Xanthomonas Citri Complexed with Glucose-1-Phosphate, PDB code: 5bmp:

Magnesium binding site 1 out of 1 in 5bmp

Go back to Magnesium Binding Sites List in 5bmp
Magnesium binding site 1 out of 1 in the Crystal Structure of Phosphoglucomutase From Xanthomonas Citri Complexed with 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 Phosphoglucomutase From Xanthomonas Citri Complexed with Glucose-1-Phosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:14.9
occ:1.00
 O1P A:SEP119 1.9 69.1 1.0
OD2 A:ASP259 2.1 9.2 1.0
OD1 A:ASP261 2.1 11.4 1.0
OD1 A:ASP263 2.1 10.8 1.0
OD2 A:ASP261 2.7 11.7 1.0
CG A:ASP261 2.8 10.3 1.0
P A:SEP119 3.0 47.0 1.0
CG A:ASP259 3.0 9.8 1.0
CG A:ASP263 3.1 12.0 1.0
OG A:SEP119 3.1 35.0 1.0
OD2 A:ASP263 3.3 14.7 1.0
OD1 A:ASP259 3.4 9.2 1.0
NZ A:LYS129 3.9 25.9 1.0
O2P A:SEP119 4.0 30.2 1.0
O3P A:SEP119 4.1 42.6 1.0
CB A:SEP119 4.2 32.0 1.0
NE A:ARG264 4.2 21.1 1.0
CB A:ASP261 4.2 7.8 1.0
N A:ASP263 4.3 6.3 1.0
CB A:ASP259 4.3 6.8 1.0
CB A:ASP263 4.4 8.8 1.0
CG A:ARG264 4.6 8.8 1.0
N A:ARG264 4.6 5.9 1.0
N A:ASP261 4.6 7.5 1.0
CA A:ASP263 4.8 6.2 1.0
CA A:SEP119 4.8 27.6 1.0
CA A:ASP261 4.8 7.5 1.0
C A:ASP261 4.8 7.0 1.0
N A:PHE262 4.9 6.7 1.0
NH2 A:ARG264 4.9 26.2 1.0
C A:ASP263 4.9 8.7 1.0
CD A:ARG264 5.0 14.3 1.0
CB A:ARG264 5.0 7.1 1.0

Reference:

L.S.Goto, A.Vessoni Alexandrino, C.Malvessi Pereira, C.Silva Martins, H.D'muniz Pereira, J.Brandao-Neto, M.T.Marques Novo-Mansur. Structural and Functional Characterization of the Phosphoglucomutase From Xanthomonas Citri Subsp. Citri. Biochim.Biophys.Acta V.1864 1658 2016.
ISSN: ISSN 0006-3002
PubMed: 27567706
DOI: 10.1016/J.BBAPAP.2016.08.014
Page generated: Tue Aug 12 05:41:33 2025

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