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Magnesium in PDB 7b4q: Structure of A Cold Active Hsl Family Esterase Reveals Mechanisms of Low Temperature Adaptation and Substrate Specificity

Enzymatic activity of Structure of A Cold Active Hsl Family Esterase Reveals Mechanisms of Low Temperature Adaptation and Substrate Specificity

All present enzymatic activity of Structure of A Cold Active Hsl Family Esterase Reveals Mechanisms of Low Temperature Adaptation and Substrate Specificity:
3.1.1.3;

Protein crystallography data

The structure of Structure of A Cold Active Hsl Family Esterase Reveals Mechanisms of Low Temperature Adaptation and Substrate Specificity, PDB code: 7b4q was solved by P.J.Rizkallah, D.D.Jones, N.Noby, H.Auhim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 83.03 / 1.61
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 109.883, 109.883, 126.772, 90, 90, 90
R / Rfree (%) 16.7 / 19.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of A Cold Active Hsl Family Esterase Reveals Mechanisms of Low Temperature Adaptation and Substrate Specificity (pdb code 7b4q). 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 A Cold Active Hsl Family Esterase Reveals Mechanisms of Low Temperature Adaptation and Substrate Specificity, PDB code: 7b4q:

Magnesium binding site 1 out of 1 in 7b4q

Go back to Magnesium Binding Sites List in 7b4q
Magnesium binding site 1 out of 1 in the Structure of A Cold Active Hsl Family Esterase Reveals Mechanisms of Low Temperature Adaptation and Substrate Specificity


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of A Cold Active Hsl Family Esterase Reveals Mechanisms of Low Temperature Adaptation and Substrate Specificity within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg404

b:30.6
occ:1.00
 O A:HOH617 2.1 36.5 1.0
O A:HOH574 2.1 28.5 1.0
O A:HOH532 2.1 48.9 1.0
O A:HOH697 4.1 46.5 1.0
O A:HOH524 4.1 29.3 1.0
OE2 A:GLU212 4.1 29.9 1.0
O A:LYS191 4.2 22.4 1.0
O A:HOH686 4.3 36.7 1.0
O A:HOH690 4.3 46.9 1.0
OE1 A:GLU212 4.3 27.6 1.0
CD A:GLU212 4.7 28.9 1.0

Reference:

N.Noby, H.S.Auhim, S.Winter, H.L.Worthy, A.M.Embaby, H.Saeed, A.Hussein, C.R.Pudney, P.J.Rizkallah, S.A.Wells, D.D.Jones. Structure and in Silico Simulations of A Cold-Active Esterase Reveals Its Prime Cold-Adaptation Mechanism. Open Biology V. 11 10182 2021.
ISSN: ESSN 2046-2441
PubMed: 34847772
DOI: 10.1098/RSOB.210182
Page generated: Wed Oct 2 10:19:16 2024

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