Magnesium in PDB 5hm7: The Intracellular Domain of Butyrophilin 3A1 Protein

The structure of The Intracellular Domain of Butyrophilin 3A1 Protein, PDB code: 5hm7 was solved by E.J.Adams, S.Gu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	72.92 / 1.93
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	37.430, 145.840, 44.910, 90.00, 105.57, 90.00
R / Rfree (%)	19.7 / 22.7

The binding sites of Magnesium atom in the The Intracellular Domain of Butyrophilin 3A1 Protein (pdb code 5hm7). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The Intracellular Domain of Butyrophilin 3A1 Protein, PDB code: 5hm7:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the The Intracellular Domain of Butyrophilin 3A1 Protein


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Intracellular Domain of Butyrophilin 3A1 Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg504 b:28.5 occ:1.00 O A:TRP350 2.7 11.0 1.0 O3 A:GOL501 2.7 18.6 1.0 CD2 A:TRP350 3.2 16.6 1.0 O A:HOH662 3.3 34.0 1.0 CE2 A:TRP350 3.3 15.8 1.0 CE1 A:TYR352 3.4 15.9 1.0 CE3 A:TRP350 3.5 14.0 1.0 C A:TRP350 3.6 13.2 1.0 CG A:TRP350 3.6 14.3 1.0 CZ2 A:TRP350 3.7 14.4 1.0 NE1 A:TRP350 3.7 18.1 1.0 O A:HOH619 3.8 32.4 1.0 C3 A:GOL501 3.8 33.4 1.0 CZ3 A:TRP350 3.9 13.3 1.0 CA A:TRP350 3.9 12.5 1.0 CD1 A:TRP350 3.9 17.4 1.0 CH2 A:TRP350 4.0 14.6 1.0 CD1 A:TYR352 4.0 16.4 1.0 C2 A:GOL501 4.0 31.9 1.0 CZ A:TYR352 4.2 16.9 1.0 OH A:TYR352 4.4 12.9 1.0 CB A:TRP350 4.4 13.1 1.0 N A:HIS351 4.7 11.1 1.0 C1 A:GOL501 4.9 32.0 1.0

Magnesium binding site 2 out of 2 in the The Intracellular Domain of Butyrophilin 3A1 Protein


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The Intracellular Domain of Butyrophilin 3A1 Protein within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg505 b:23.0 occ:1.00 O B:TRP350 2.5 11.5 1.0 O1 B:GOL501 2.6 21.3 1.0 CD2 B:TRP350 3.2 11.9 1.0 CE2 B:TRP350 3.3 13.0 1.0 O B:HOH633 3.3 25.9 1.0 CE1 B:TYR352 3.4 18.2 1.0 C B:TRP350 3.4 13.5 1.0 C1 B:GOL501 3.4 28.2 1.0 CB A:SER326 3.5 10.3 1.0 CE3 B:TRP350 3.5 13.7 1.0 CG B:TRP350 3.6 13.1 1.0 NE1 B:TRP350 3.7 15.4 1.0 CA B:TRP350 3.8 11.7 1.0 CZ2 B:TRP350 3.8 12.3 1.0 C2 B:GOL501 3.8 26.0 1.0 CD1 B:TRP350 3.9 15.3 1.0 CZ3 B:TRP350 3.9 15.0 1.0 CD1 B:TYR352 3.9 14.7 1.0 O B:HOH619 4.0 27.9 1.0 CA A:SER326 4.0 10.2 1.0 CH2 B:TRP350 4.1 13.0 1.0 CB B:TRP350 4.3 12.4 1.0 CZ B:TYR352 4.3 16.7 1.0 OH B:TYR352 4.5 15.1 1.0 N B:HIS351 4.6 14.6 1.0 O2 B:GOL501 4.8 32.0 1.0 OG A:SER326 4.8 11.2 1.0 N A:GLU327 4.8 13.3 1.0 C3 B:GOL501 4.8 29.4 1.0 ND2 B:ASN320 4.9 20.0 1.0

S.Gu, J.R.Sachleben, C.T.Boughter, W.I.Nawrocka, M.T.Borowska, J.T.Tarrasch, G.Skiniotis, B.Roux, E.J.Adams. Phosphoantigen-Induced Conformational Change of Butyrophilin 3A1 (BTN3A1) and Its Implication on V Gamma 9V Delta 2 T Cell Activation. Proc. Natl. Acad. Sci. V. 114 E7311 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28807997
DOI: 10.1073/PNAS.1707547114