Magnesium in PDB 5zfx: Crystal Structure of Triosephosphate Isomerase From Opisthorchis Viverrini

All present enzymatic activity of Crystal Structure of Triosephosphate Isomerase From Opisthorchis Viverrini:
5.3.1.1;

The structure of Crystal Structure of Triosephosphate Isomerase From Opisthorchis Viverrini, PDB code: 5zfx was solved by J.Son, S.Kim, S.E.Kim, H.Lee, M.R.Lee, K.Y.Hwang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.08 / 1.75
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	96.529, 206.621, 97.466, 90.00, 90.00, 90.00
R / Rfree (%)	16.4 / 20

The binding sites of Magnesium atom in the Crystal Structure of Triosephosphate Isomerase From Opisthorchis Viverrini (pdb code 5zfx). 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 Triosephosphate Isomerase From Opisthorchis Viverrini, PDB code: 5zfx:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Triosephosphate Isomerase From Opisthorchis Viverrini


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 Triosephosphate Isomerase From Opisthorchis Viverrini within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:34.9 occ:1.00 O B:HOH559 2.1 36.9 1.0 O B:HOH433 2.2 34.1 1.0 NE2 B:HIS31 2.2 23.2 1.0 OE1 B:GLU27 2.2 39.0 1.0 CE1 B:HIS31 3.1 30.4 1.0 CD B:GLU27 3.2 42.6 1.0 CD2 B:HIS31 3.2 25.6 1.0 OE2 B:GLU27 3.4 44.7 1.0 ND1 B:HIS31 4.3 24.5 1.0 CG B:HIS31 4.4 21.1 1.0 O B:HOH638 4.5 40.0 1.0 CG B:GLU27 4.5 34.1 1.0 O B:HOH722 4.8 72.0 1.0 CB B:GLU27 4.9 21.0 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Triosephosphate Isomerase From Opisthorchis Viverrini


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 Triosephosphate Isomerase From Opisthorchis Viverrini within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg302 b:14.7 occ:1.00 O B:LYS178 2.3 16.5 1.0 O B:ALA173 2.3 12.9 1.0 O B:THR176 2.4 13.5 1.0 O B:HOH477 2.5 21.1 1.0 O B:HOH649 2.5 25.0 1.0 O B:HOH643 2.5 19.7 1.0 C B:ALA173 3.4 14.6 1.0 C B:LYS178 3.4 16.6 1.0 C B:THR176 3.5 11.5 1.0 N B:LYS178 3.7 16.0 1.0 C B:GLY177 3.8 20.9 1.0 CA B:GLY177 4.1 16.4 1.0 O B:ILE174 4.2 12.8 1.0 CA B:LYS178 4.2 15.8 1.0 CA B:ALA173 4.2 10.8 1.0 N B:GLY177 4.3 12.9 1.0 N B:ILE174 4.3 12.9 1.0 C B:ILE174 4.3 14.3 1.0 O B:GLY177 4.4 18.1 1.0 N B:THR176 4.4 11.2 1.0 CA B:ILE174 4.4 10.9 1.0 N B:THR179 4.5 19.1 1.0 CA B:THR176 4.6 12.8 1.0 O B:HOH710 4.6 36.2 1.0 CB B:ALA173 4.6 12.4 1.0 OG1 B:THR176 4.6 13.2 1.0 CA B:THR179 4.7 19.2 1.0 O B:HOH602 4.7 20.9 1.0 CG2 B:THR179 4.8 23.7 1.0

J.Son, S.Kim, S.E.Kim, H.Lee, M.R.Lee, K.Y.Hwang. Structural Analysis of An Epitope Candidate of Triosephosphate Isomerase in Opisthorchis Viverrini. Sci Rep V. 8 15075 2018.
ISSN: ESSN 2045-2322
PubMed: 30305716
DOI: 10.1038/S41598-018-33479-8