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Magnesium in PDB 5o6p: Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1,6-Bisphosphate

Enzymatic activity of Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1,6-Bisphosphate

All present enzymatic activity of Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1,6-Bisphosphate:
5.4.2.6;

Protein crystallography data

The structure of Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1,6-Bisphosphate, PDB code: 5o6p was solved by M.W.Bowler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 31.750, 68.300, 83.230, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 25.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1,6-Bisphosphate (pdb code 5o6p). 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 Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1,6-Bisphosphate, PDB code: 5o6p:

Magnesium binding site 1 out of 1 in 5o6p

Go back to Magnesium Binding Sites List in 5o6p
Magnesium binding site 1 out of 1 in the Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1,6-Bisphosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1,6-Bisphosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg302

b:23.4
occ:1.00
 O1X A:B16301 2.0 22.1 1.0
OD2 A:ASP8 2.1 23.1 1.0
O A:HOH444 2.1 19.5 1.0
O A:HOH433 2.1 27.2 1.0
O A:ASN10 2.1 19.0 1.0
OD1 A:ASP170 2.6 22.2 1.0
CG A:ASP8 3.0 22.5 1.0
OD1 A:ASP8 3.2 22.8 1.0
C A:ASN10 3.3 18.3 1.0
P' A:B16301 3.5 25.3 1.0
CG A:ASP170 3.6 22.4 1.0
O2 A:B16301 3.8 23.9 1.0
OD2 A:ASP170 3.8 25.1 1.0
OE1 A:GLU169 4.0 17.6 1.0
O2X A:B16301 4.0 31.2 1.0
CB A:ASN10 4.1 18.4 1.0
CA A:ASN10 4.1 18.0 1.0
N A:ASN10 4.1 17.9 1.0
O3X A:B16301 4.2 22.7 1.0
N A:GLY46 4.3 37.2 1.0
N A:GLY11 4.4 17.8 1.0
CB A:ASP8 4.4 20.6 1.0
O1 A:B16301 4.5 28.7 1.0
CA A:GLY46 4.6 35.3 1.0
CA A:GLY11 4.6 18.8 1.0
CD A:GLU169 4.8 17.2 1.0
OE2 A:GLU169 4.8 17.4 1.0
NZ A:LYS145 4.9 17.0 1.0
CB A:ASP170 5.0 20.8 1.0
CB A:SER171 5.0 24.9 1.0
C2 A:B16301 5.0 26.8 1.0

Reference:

L.A.Johnson, A.J.Robertson, N.J.Baxter, C.R.Trevitt, C.Bisson, Y.Jin, H.P.Wood, A.M.Hounslow, M.J.Cliff, G.M.Blackburn, M.W.Bowler, J.P.Waltho. Van Der Waals Contact Between Nucleophile and Transferring Phosphorus Is Insufficient to Achieve Enzyme Transition-State Architecture Acs Catalysis 2018.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.8B01612
Page generated: Mon Sep 30 00:12:22 2024

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