Magnesium in PDB 8jnu: Crystal Structure of V30G Mutated Human Transthyretin

The structure of Crystal Structure of V30G Mutated Human Transthyretin, PDB code: 8jnu was solved by M.Mizuguchi, S.Yamada, T.Obita, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.60 / 1.64
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	43.1, 85.4, 64.48, 90, 90, 90
R / Rfree (%)	18.5 / 20.7

The binding sites of Magnesium atom in the Crystal Structure of V30G Mutated Human Transthyretin (pdb code 8jnu). 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 V30G Mutated Human Transthyretin, PDB code: 8jnu:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of V30G Mutated Human Transthyretin


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 V30G Mutated Human Transthyretin within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg201 b:32.5 occ:1.00 O A:HOH318 2.0 29.9 1.0 O A:HOH303 2.1 27.4 1.0 O A:HOH349 2.2 35.2 1.0 OE2 A:GLU66 3.7 26.2 1.0 OE1 A:GLU66 4.0 21.2 1.0 CD A:GLU66 4.2 24.9 1.0 OD1 A:ASN98 4.3 36.2 1.0 O A:HOH364 4.4 43.1 1.0 O A:HOH355 4.9 32.4 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of V30G Mutated Human Transthyretin


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 V30G Mutated Human Transthyretin within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg201 b:23.5 occ:1.00 O B:HOH313 2.0 24.7 1.0 O B:HOH305 2.1 25.5 1.0 OE1 B:GLU66 3.8 25.5 1.0 OE2 B:GLU66 3.9 22.5 1.0 O B:ASP99 4.2 33.6 1.0 CD B:GLU66 4.3 21.7 1.0 OD1 B:ASP99 4.5 39.0 1.0 O B:HOH352 4.7 29.9 1.0

M.Mizuguchi, T.Obita, S.Yamada, Y.Nabeshima. Trypsin-Induced Aggregation of Transthyretin Valine 30 Variants Associated with Hereditary Amyloidosis. Febs J. 2024.
ISSN: ISSN 1742-464X
PubMed: 38273457
DOI: 10.1111/FEBS.17070