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Magnesium in PDB 5ok1: D10N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Trapped with Native Beta-Glucose 1,6-Bisphosphate Intermediate to 1.9A Resolution.

Enzymatic activity of D10N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Trapped with Native Beta-Glucose 1,6-Bisphosphate Intermediate to 1.9A Resolution.

All present enzymatic activity of D10N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Trapped with Native Beta-Glucose 1,6-Bisphosphate Intermediate to 1.9A Resolution.:
5.4.2.6;

Protein crystallography data

The structure of D10N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Trapped with Native Beta-Glucose 1,6-Bisphosphate Intermediate to 1.9A Resolution., PDB code: 5ok1 was solved by A.J.Robertson, C.Bisson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.28 / 1.86
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 36.710, 74.490, 78.560, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 24.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the D10N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Trapped with Native Beta-Glucose 1,6-Bisphosphate Intermediate to 1.9A Resolution. (pdb code 5ok1). 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 D10N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Trapped with Native Beta-Glucose 1,6-Bisphosphate Intermediate to 1.9A Resolution., PDB code: 5ok1:

Magnesium binding site 1 out of 1 in 5ok1

Go back to Magnesium Binding Sites List in 5ok1
Magnesium binding site 1 out of 1 in the D10N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Trapped with Native Beta-Glucose 1,6-Bisphosphate Intermediate to 1.9A Resolution.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of D10N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Trapped with Native Beta-Glucose 1,6-Bisphosphate Intermediate to 1.9A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:37.5
occ:1.00
 O A:HOH406 1.9 37.0 1.0
O2X A:B16302 2.0 33.8 1.0
O A:HOH435 2.1 30.3 1.0
O A:ASN10 2.2 34.2 1.0
OD2 A:ASP8 2.2 36.5 1.0
OD1 A:ASP170 2.6 41.6 1.0
OD1 A:ASP8 2.8 37.7 1.0
CG A:ASP8 2.8 35.5 1.0
C A:ASN10 3.3 30.0 1.0
P' A:B16302 3.4 34.9 1.0
CG A:ASP170 3.7 39.0 1.0
OE1 A:GLU169 3.9 40.5 1.0
O3X A:B16302 4.0 33.3 1.0
CA A:ASN10 4.0 30.2 1.0
O1X A:B16302 4.0 31.0 1.0
CB A:ASN10 4.1 29.7 1.0
N A:ASN10 4.1 29.2 1.0
OD2 A:ASP170 4.1 51.5 1.0
O2 A:B16302 4.1 32.9 1.0
O A:HOH453 4.2 40.6 1.0
CB A:ASP8 4.3 32.7 1.0
N A:GLY11 4.4 28.4 1.0
OE2 A:GLU169 4.5 39.9 1.0
OG A:SER171 4.5 40.7 1.0
CD A:GLU169 4.5 38.2 1.0
O1 A:B16302 4.6 37.3 1.0
N A:GLY46 4.7 39.8 1.0
NZ A:LYS145 4.8 37.8 1.0
CA A:GLY11 4.8 31.1 1.0
C A:LEU9 4.8 30.0 1.0
CB A:SER171 4.9 40.5 1.0
CA A:GLY46 4.9 37.7 1.0
CB A:ASP170 4.9 39.1 1.0
N A:LEU9 5.0 31.2 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 01:01:33 2024

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