Magnesium in PDB 9h4e: Trans-Aconitate Decarboxylase TAD1- Wild Type Binding with Glycerol

All present enzymatic activity of Trans-Aconitate Decarboxylase TAD1- Wild Type Binding with Glycerol:
4.1.1.113;

The structure of Trans-Aconitate Decarboxylase TAD1- Wild Type Binding with Glycerol, PDB code: 9h4e was solved by L.Zheng, G.Bang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.81 / 2.35
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	153.67, 160.83, 209.56, 90, 90, 90
R / Rfree (%)	22.7 / 25.3

The binding sites of Magnesium atom in the Trans-Aconitate Decarboxylase TAD1- Wild Type Binding with Glycerol (pdb code 9h4e). 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 Trans-Aconitate Decarboxylase TAD1- Wild Type Binding with Glycerol, PDB code: 9h4e:

Magnesium binding site 1 out of 1 in the Trans-Aconitate Decarboxylase TAD1- Wild Type Binding with Glycerol


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Trans-Aconitate Decarboxylase TAD1- Wild Type Binding with Glycerol within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg502 b:53.6 occ:1.00 ND1 B:HIS272 2.8 50.3 1.0 O B:GLU359 2.9 54.8 1.0 NH1 D:ARG213 2.9 40.9 1.0 C B:ALA241 3.1 49.6 1.0 O B:ALA241 3.3 53.2 1.0 NH2 D:ARG213 3.4 49.9 1.0 CA B:ALA241 3.4 46.3 1.0 N B:GLY242 3.5 49.0 1.0 CZ D:ARG213 3.6 47.3 1.0 CG B:HIS272 3.7 55.5 1.0 CD B:ARG360 3.7 65.8 1.0 CB B:GLU359 3.7 50.7 1.0 C B:GLU359 3.7 53.7 1.0 CB B:HIS272 3.7 51.5 1.0 CE1 B:HIS272 3.8 52.4 1.0 O B:ALA240 3.9 56.2 1.0 CA B:GLY242 4.0 48.0 1.0 CA B:GLU359 4.1 51.5 1.0 CG B:ARG360 4.1 63.0 1.0 N B:ALA241 4.3 53.2 1.0 CG B:GLU359 4.4 46.3 1.0 C B:ALA240 4.4 52.2 1.0 O B:GLY239 4.6 52.2 1.0 CB B:ALA241 4.6 45.5 1.0 N B:ARG360 4.8 49.1 1.0 NE B:ARG360 4.9 71.7 1.0 CD2 B:HIS272 4.9 48.7 1.0 NE D:ARG213 4.9 46.3 1.0 NE2 B:HIS272 4.9 50.0 1.0 CA B:HIS272 5.0 48.5 1.0 N B:HIS272 5.0 51.1 1.0 CB B:ALA270 5.0 36.8 1.0

L.Zheng, W.Li, M.Christ, N.Paczia, W.Buckel, C.N.Mais, M.Bolker, J.Freitag, G.Bange. Mechanistic and Structural Insights Into the Itaconate-Producing Trans -Aconitate Decarboxylase TAD1. PNAS Nexus V. 4 AF059 2025.
ISSN: ESSN 2752-6542
PubMed: 40045995
DOI: 10.1093/PNASNEXUS/PGAF059