Magnesium in PDB 8bp1: Crystal Structure of BHMEHIS1.0, An Engineered Enzyme For the Morita- Baylis-Hillman Reaction

The structure of Crystal Structure of BHMEHIS1.0, An Engineered Enzyme For the Morita- Baylis-Hillman Reaction, PDB code: 8bp1 was solved by F.J.Hardy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	61.50 / 1.72
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	71.013, 71.013, 120.312, 90, 90, 120
R / Rfree (%)	18.1 / 20.2

The binding sites of Magnesium atom in the Crystal Structure of BHMEHIS1.0, An Engineered Enzyme For the Morita- Baylis-Hillman Reaction (pdb code 8bp1). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of BHMEHIS1.0, An Engineered Enzyme For the Morita- Baylis-Hillman Reaction, PDB code: 8bp1:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of BHMEHIS1.0, An Engineered Enzyme For the Morita- Baylis-Hillman Reaction


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 BHMEHIS1.0, An Engineered Enzyme For the Morita- Baylis-Hillman Reaction within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg304 b:26.8 occ:1.00 O A:HOH530 2.0 30.0 1.0 OD1 A:ASP180 2.1 28.9 1.0 O A:HOH438 2.1 29.1 1.0 O A:HOH436 2.1 27.4 1.0 OD2 A:ASP8 2.1 27.0 1.0 O A:LEU10 2.1 29.1 1.0 CG A:ASP8 3.0 28.5 1.0 CG A:ASP180 3.1 33.9 1.0 OD1 A:ASP8 3.3 26.7 1.0 C A:LEU10 3.3 30.2 1.0 HB3 A:LEU10 3.4 35.2 1.0 OD2 A:ASP180 3.5 36.5 1.0 HG1 A:THR12 3.5 33.3 1.0 H A:ASP180 3.7 35.4 1.0 O4 A:SO4306 4.0 34.6 0.8 OD2 A:ASP185 4.0 29.4 1.0 CA A:LEU10 4.0 28.5 1.0 H A:LEU10 4.0 31.6 1.0 N A:LEU10 4.1 26.3 1.0 HA3 A:GLY11 4.1 33.9 1.0 CB A:LEU10 4.2 29.3 1.0 O1 A:SO4306 4.2 34.3 0.8 HZ1 A:LYS155 4.2 42.4 1.0 OG1 A:THR12 4.3 27.7 1.0 N A:GLY11 4.3 27.7 1.0 HB2 A:ASN181 4.4 41.2 1.0 CB A:ASP8 4.4 27.2 1.0 CB A:ASP180 4.4 33.9 1.0 HB3 A:ASP8 4.5 32.8 1.0 HG A:LEU10 4.5 38.8 1.0 N A:ASP180 4.5 29.4 1.0 S A:SO4306 4.5 35.5 0.8 H A:SER9 4.6 31.1 1.0 O2 A:SO4306 4.6 39.5 0.8 H A:THR12 4.6 31.4 1.0 CA A:GLY11 4.6 28.2 1.0 C A:SER9 4.7 28.2 1.0 HB3 A:ASP180 4.7 40.7 1.0 H A:ASN181 4.7 35.2 1.0 HB2 A:ASP8 4.8 32.8 1.0 N A:THR12 4.9 26.1 1.0 CG A:LEU10 4.9 32.3 1.0 HB2 A:LEU10 4.9 35.2 1.0 CA A:ASP180 4.9 32.8 1.0 N A:SER9 4.9 25.8 1.0 HD23 A:LEU10 4.9 39.4 1.0 HA A:LEU10 4.9 34.2 1.0 NZ A:LYS155 4.9 35.2 1.0 C A:GLY11 4.9 27.8 1.0 N A:ASN181 5.0 29.7 1.0 HZ3 A:LYS155 5.0 42.4 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of BHMEHIS1.0, An Engineered Enzyme For the Morita- Baylis-Hillman Reaction


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of BHMEHIS1.0, An Engineered Enzyme For the Morita- Baylis-Hillman Reaction within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg305 b:43.2 occ:1.00 H A:ASN123 2.0 32.2 1.0 O2 A:SO4306 2.6 39.5 0.8 HB2 A:ASN123 2.8 49.4 1.0 OG A:SER9 2.8 35.9 1.0 N A:ASN123 2.9 26.8 1.0 HG A:SER9 2.9 43.2 1.0 HA A:LEU122 3.0 30.6 1.0 HB3 A:ASN123 3.1 49.4 1.0 CB A:ASN123 3.3 41.1 1.0 HZ3 A:LYS155 3.4 42.4 1.0 O A:HOH404 3.4 44.3 1.0 O A:HOH436 3.5 27.4 1.0 HG2 A:ARG124 3.5 41.6 1.0 OD1 A:ASP8 3.7 26.7 1.0 CA A:ASN123 3.7 29.8 1.0 HH12 A:ARG124 3.7 57.6 1.0 NH1 A:ARG124 3.7 47.9 1.0 H A:SER9 3.7 31.1 1.0 CZ A:ARG124 3.7 59.2 1.0 S A:SO4306 3.8 35.5 0.8 CA A:LEU122 3.8 25.4 1.0 HH22 A:ARG124 3.8 66.3 1.0 C A:LEU122 3.8 29.9 1.0 NH2 A:ARG124 3.8 55.2 1.0 O4 A:SO4306 3.9 34.6 0.8 H A:LEU10 4.0 31.6 1.0 HH11 A:ARG124 4.0 57.6 1.0 HZ1 A:LYS155 4.1 42.4 1.0 NZ A:LYS155 4.1 35.2 1.0 O A:ILE121 4.1 28.2 1.0 CB A:SER9 4.2 33.8 1.0 HH21 A:ARG124 4.2 66.3 1.0 HD23 A:LEU122 4.2 37.9 1.0 C A:ASN123 4.3 34.1 1.0 HE2 A:LYS155 4.3 51.4 1.0 O1 A:PEG301 4.3 48.8 1.0 NE A:ARG124 4.3 50.5 1.0 HB3 A:LEU122 4.3 34.6 1.0 CG A:ARG124 4.4 34.6 1.0 O3 A:SO4306 4.4 37.7 0.8 HB3 A:SER9 4.4 40.7 1.0 HG3 A:ARG124 4.4 41.6 1.0 HO1 A:PEG301 4.5 58.6 1.0 HA A:ASN123 4.5 35.8 1.0 N A:SER9 4.5 25.8 1.0 O A:ASN123 4.6 42.3 1.0 CB A:LEU122 4.7 28.8 1.0 HE A:ARG124 4.7 60.7 1.0 CG A:ASN123 4.7 35.2 1.0 CE A:LYS155 4.7 42.8 1.0 HD3 A:LYS155 4.8 57.9 1.0 HZ2 A:LYS155 4.8 42.4 1.0 N A:LEU10 4.8 26.3 1.0 HB2 A:SER9 4.8 40.7 1.0 N A:LEU122 4.8 24.1 1.0 HD22 A:ASN123 4.8 42.8 1.0 CG A:ASP8 4.8 28.5 1.0 CD A:ARG124 4.9 37.0 1.0 O1 A:SO4306 4.9 34.3 0.8 HB3 A:LEU10 4.9 35.2 1.0 C A:ILE121 4.9 29.1 1.0 CA A:SER9 4.9 24.6 1.0

A.E.Hutton, A.E.Crossley. A Non-Canonical Nucleophile Unlocks A New Mechanistic Pathway in A Designed Enzyme To Be Published 2024.
DOI: 10.1038/S41467-024-46123-Z