Magnesium in PDB 4eo7: Crystal Structure of the Tir Domain of Human Myeloid Differentiation Primary Response Protein 88.

The structure of Crystal Structure of the Tir Domain of Human Myeloid Differentiation Primary Response Protein 88., PDB code: 4eo7 was solved by G.A.Snyder, C.Cirl, J.S.Jiang, P.Chen, T.Smith, T.S.Xiao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.24 / 1.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	34.876, 56.810, 66.664, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / 20.8

The binding sites of Magnesium atom in the Crystal Structure of the Tir Domain of Human Myeloid Differentiation Primary Response Protein 88. (pdb code 4eo7). 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 Crystal Structure of the Tir Domain of Human Myeloid Differentiation Primary Response Protein 88., PDB code: 4eo7:

Magnesium binding site 1 out of 1 in the Crystal Structure of the Tir Domain of Human Myeloid Differentiation Primary Response Protein 88.


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 the Tir Domain of Human Myeloid Differentiation Primary Response Protein 88. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:11.7 occ:1.00 NZ A:LYS282 3.1 9.5 1.0 CA A:PRO279 3.5 7.3 0.9 CG A:LYS282 3.6 6.4 0.9 CB A:LYS282 3.7 5.8 1.0 CB A:PRO279 3.8 8.8 0.7 CE A:LYS282 4.1 8.6 1.0 N A:PRO279 4.1 8.9 1.0 O A:HOH412 4.3 10.4 1.0 CD A:LYS282 4.4 8.2 1.0 C A:ASN278 4.6 8.7 1.0 O A:TYR276 4.7 9.8 1.0 O A:ASN278 4.7 6.3 0.8 CD A:PRO279 4.7 11.0 1.0 C A:PRO279 4.7 7.9 0.7 CG A:PRO279 4.8 19.2 1.0 O A:PRO279 4.9 10.1 1.0

G.A.Snyder, C.Cirl, J.Jiang, K.Chen, A.Waldhuber, P.Smith, F.Rommler, N.Snyder, T.Fresquez, S.Durr, N.Tjandra, T.Miethke, T.S.Xiao. Molecular Mechanisms For the Subversion of MYD88 Signaling By Tcpc From Virulent Uropathogenic Escherichia Coli. Proc.Natl.Acad.Sci.Usa V. 110 6985 2013.
ISSN: ISSN 0027-8424
PubMed: 23569230
DOI: 10.1073/PNAS.1215770110