Magnesium in PDB 1ext: Extracellular Domain of the 55KDA Tumor Necrosis Factor Receptor. Crystallized at PH3.7 in P 21 21 21.

The structure of Extracellular Domain of the 55KDA Tumor Necrosis Factor Receptor. Crystallized at PH3.7 in P 21 21 21., PDB code: 1ext was solved by J.H.Naismith, S.R.Sprang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.85
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	78.810, 83.060, 67.900, 90.00, 90.00, 90.00
R / Rfree (%)	20.3 / 24.3

The binding sites of Magnesium atom in the Extracellular Domain of the 55KDA Tumor Necrosis Factor Receptor. Crystallized at PH3.7 in P 21 21 21. (pdb code 1ext). 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 Extracellular Domain of the 55KDA Tumor Necrosis Factor Receptor. Crystallized at PH3.7 in P 21 21 21., PDB code: 1ext:

Magnesium binding site 1 out of 1 in the Extracellular Domain of the 55KDA Tumor Necrosis Factor Receptor. Crystallized at PH3.7 in P 21 21 21.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Extracellular Domain of the 55KDA Tumor Necrosis Factor Receptor. Crystallized at PH3.7 in P 21 21 21. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg404 b:39.4 occ:1.00 O A:HOH497 2.2 22.9 1.0 OE1 A:GLU147 2.2 12.6 1.0 O B:HOH219 2.3 15.7 1.0 O B:HOH257 2.3 34.9 1.0 O B:HOH275 2.4 26.1 1.0 O A:HOH473 2.6 24.6 1.0 CD A:GLU147 3.1 11.7 1.0 OE2 A:GLU147 3.4 10.6 1.0 O A:HOH564 3.8 32.3 1.0 O B:LYS19 4.3 12.8 1.0 N A:GLU147 4.4 8.1 1.0 CA A:GLU147 4.4 9.6 1.0 CG A:GLU147 4.4 10.2 1.0 O A:HOH579 4.5 35.7 1.0 NE2 B:GLN17 4.7 44.6 1.0 CB A:GLU147 4.8 9.6 1.0 NZ B:LYS32 4.9 20.7 1.0 O B:PRO16 4.9 15.3 1.0 CD A:ARG146 5.0 6.2 1.0

J.H.Naismith, T.Q.Devine, T.Kohno, S.R.Sprang. Structures of the Extracellular Domain of the Type I Tumor Necrosis Factor Receptor. Structure V. 4 1251 1996.
ISSN: ISSN 0969-2126
PubMed: 8939750
DOI: 10.1016/S0969-2126(96)00134-7