Magnesium in PDB 9ega: Crystal Structure of A CE20 Carbohydrate Acetylesterase From Pedobacter Psychrotolerans (PPCE20_II), with Ancillary Domain

The structure of Crystal Structure of A CE20 Carbohydrate Acetylesterase From Pedobacter Psychrotolerans (PPCE20_II), with Ancillary Domain, PDB code: 9ega was solved by P.S.Vieira, M.A.B.Morais, M.T.Murakami, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.72 / 1.35
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	56.134, 125.135, 108.688, 90, 104.71, 90
R / Rfree (%)	15.9 / 19.2

The binding sites of Magnesium atom in the Crystal Structure of A CE20 Carbohydrate Acetylesterase From Pedobacter Psychrotolerans (PPCE20_II), with Ancillary Domain (pdb code 9ega). 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 A CE20 Carbohydrate Acetylesterase From Pedobacter Psychrotolerans (PPCE20_II), with Ancillary Domain, PDB code: 9ega:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of A CE20 Carbohydrate Acetylesterase From Pedobacter Psychrotolerans (PPCE20_II), with Ancillary Domain


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 A CE20 Carbohydrate Acetylesterase From Pedobacter Psychrotolerans (PPCE20_II), with Ancillary Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg702 b:18.3 occ:1.00 O A:HOH1406 2.2 17.6 1.0 O A:GLY363 2.3 18.0 1.0 OD1 A:ASN360 2.3 17.5 1.0 OD1 A:ASP288 2.4 20.9 1.0 O A:LEU287 2.4 17.6 1.0 O A:HOH1433 3.1 33.3 1.0 C A:LEU287 3.3 19.2 1.0 CG A:ASN360 3.4 16.9 1.0 C A:GLY363 3.4 17.0 1.0 CG A:ASP288 3.5 20.8 1.0 O A:HOH1418 3.6 24.4 1.0 CA A:ASP288 3.8 17.4 1.0 N A:ASP288 3.8 18.8 1.0 N A:GLY365 3.8 14.8 1.0 ND2 A:ASN360 3.9 16.2 1.0 NE1 A:TRP279 4.2 15.7 1.0 CB A:ASP288 4.2 18.1 1.0 CA A:LYS364 4.3 15.8 1.0 N A:LYS364 4.3 15.2 1.0 N A:GLY363 4.3 18.4 1.0 O A:HOH825 4.4 19.3 1.0 CA A:GLY363 4.4 17.6 1.0 O A:HOH1038 4.5 29.9 1.0 OD2 A:ASP288 4.5 23.2 1.0 C A:LYS364 4.5 15.0 1.0 N A:LEU287 4.5 19.4 1.0 CA A:LEU287 4.5 17.6 1.0 C A:ASN362 4.6 20.9 1.0 CB A:ASN360 4.7 17.0 1.0 CZ2 A:TRP279 4.7 16.2 1.0 CA A:GLY365 4.7 14.0 1.0 O A:HOH1139 4.7 15.0 1.0 CE2 A:TRP279 4.8 15.7 1.0 O A:ASN362 4.9 19.5 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of A CE20 Carbohydrate Acetylesterase From Pedobacter Psychrotolerans (PPCE20_II), with Ancillary Domain


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 A CE20 Carbohydrate Acetylesterase From Pedobacter Psychrotolerans (PPCE20_II), with Ancillary Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg701 b:15.2 occ:1.00 OD1 B:ASP288 2.2 19.1 1.0 OD1 B:ASN360 2.3 14.0 1.0 O B:GLY363 2.3 16.1 1.0 O B:HOH1397 2.4 15.2 1.0 O B:LEU287 2.4 15.2 1.0 O B:HOH1193 2.9 30.3 1.0 C B:LEU287 3.3 14.8 1.0 CG B:ASN360 3.4 12.1 1.0 CG B:ASP288 3.4 20.8 1.0 C B:GLY363 3.5 16.6 1.0 CA B:ASP288 3.7 15.1 1.0 N B:ASP288 3.8 13.5 1.0 O B:HOH1451 3.8 24.2 1.0 N B:GLY365 3.9 12.6 1.0 ND2 B:ASN360 3.9 12.4 1.0 CB B:ASP288 4.1 15.0 1.0 NE1 B:TRP279 4.2 13.4 1.0 CA B:LYS364 4.3 14.7 1.0 N B:LYS364 4.3 15.4 1.0 OD2 B:ASP288 4.4 22.3 1.0 N B:GLY363 4.4 16.0 1.0 O B:HOH831 4.4 17.6 1.0 CA B:GLY363 4.5 16.0 1.0 C B:LYS364 4.5 14.2 1.0 CA B:LEU287 4.6 14.0 1.0 N B:LEU287 4.6 15.3 1.0 C B:ASN362 4.6 16.4 1.0 CB B:ASN360 4.6 13.1 1.0 CZ2 B:TRP279 4.7 13.4 1.0 O B:HOH1223 4.7 25.3 1.0 CE2 B:TRP279 4.8 12.9 1.0 CA B:GLY365 4.8 13.5 1.0 O B:HOH1104 4.8 12.1 1.0 O B:ASN362 4.9 18.2 1.0

M.Teune, P.S.Vieira, T.Dohler, G.J.Palm, T.Dutschei, D.Bartosik, L.Berndt, G.F.Persinoti, S.Maass, D.Becher, T.Schweder, M.T.Murakami, M.Lammers, U.T.Bornscheuer. Insights Into A Water-Mediated Catalytic Triad Architecture in CE20 Carbohydrate Esterases. Nat Commun V. 16 7034 2025.
ISSN: ESSN 2041-1723
PubMed: 40745183
DOI: 10.1038/S41467-025-62387-5