Magnesium in PDB 7kc5: X-Ray Structure of Lfa-1 I Domain in Complex with Bms-68852 Collected at 273 K

The structure of X-Ray Structure of Lfa-1 I Domain in Complex with Bms-68852 Collected at 273 K, PDB code: 7kc5 was solved by R.A.Woldeyes, K.K.Hallenbeck, S.J.Pfaff, G.Lee, S.V.Cortez, M.J.Kelly, K.Akassoglou, M.R.Arkin, J.S.Fraser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	66.65 / 1.86
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	36.514, 75.412, 133.294, 90, 90, 90
R / Rfree (%)	15.9 / 21.6

The structure of X-Ray Structure of Lfa-1 I Domain in Complex with Bms-68852 Collected at 273 K also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

The binding sites of Magnesium atom in the X-Ray Structure of Lfa-1 I Domain in Complex with Bms-68852 Collected at 273 K (pdb code 7kc5). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the X-Ray Structure of Lfa-1 I Domain in Complex with Bms-68852 Collected at 273 K, PDB code: 7kc5:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the X-Ray Structure of Lfa-1 I Domain in Complex with Bms-68852 Collected at 273 K


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of X-Ray Structure of Lfa-1 I Domain in Complex with Bms-68852 Collected at 273 K within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:49.1 occ:1.00 OG1 A:THR206 2.1 14.9 1.0 OD2 A:ASP137 2.6 39.1 0.4 HG23 A:THR206 2.7 24.6 1.0 OG A:SER139 2.7 21.2 0.5 OD1 A:ASP137 2.8 28.3 0.4 HG A:SER139 2.8 25.4 0.5 OD1 A:ASP239 2.9 20.2 1.0 CG A:ASP137 3.0 22.6 0.4 HG21 A:THR206 3.0 24.6 1.0 OD2 A:ASP137 3.0 18.3 0.6 HB2 A:SER139 3.0 26.2 0.5 CG2 A:THR206 3.1 20.6 1.0 CB A:THR206 3.1 11.1 1.0 CG A:ASP137 3.4 24.5 0.6 CE A:MET140 3.6 55.1 1.0 HA A:THR206 3.6 15.2 1.0 OD1 A:ASP137 3.7 18.4 0.6 H A:SER139 3.7 29.4 0.5 H A:SER139 3.7 29.4 0.5 O A:LEU205 3.7 18.6 1.0 HA3 A:GLY240 3.7 21.8 1.0 O A:HOH561 3.8 37.9 1.0 HB A:THR206 3.8 13.3 1.0 CA A:THR206 3.9 12.7 1.0 CB A:SER139 4.0 21.9 0.5 HG A:SER139 4.0 39.3 0.5 CG A:ASP239 4.0 22.8 1.0 CB A:SER139 4.0 21.9 0.5 HG22 A:THR206 4.0 24.6 1.0 HB3 A:ASP137 4.1 21.1 0.6 H A:ASP239 4.2 15.5 1.0 HB3 A:SER139 4.2 26.3 0.5 C A:LEU205 4.2 15.3 1.0 N A:SER139 4.3 24.6 0.5 N A:SER139 4.3 24.5 0.5 CG A:MET140 4.3 45.6 1.0 OG A:SER139 4.3 32.8 0.5 N A:THR206 4.4 15.5 1.0 H A:GLY240 4.4 16.9 1.0 N A:GLY240 4.4 14.1 1.0 CB A:ASP137 4.4 17.5 0.4 CB A:ASP137 4.4 17.6 0.6 N A:MET140 4.4 23.4 1.0 CA A:GLY240 4.5 18.2 1.0 OD2 A:ASP239 4.5 29.0 1.0 O A:HOH520 4.5 25.4 1.0 HB3 A:SER139 4.6 26.2 0.5 HB2 A:ASP137 4.6 20.9 0.4 CA A:SER139 4.6 24.2 0.5 CA A:SER139 4.6 24.2 0.5 HB2 A:SER139 4.7 26.3 0.5 HB3 A:ASP137 4.7 20.9 0.4 SD A:MET140 4.7 52.2 1.0 CB A:MET140 4.7 38.3 1.0 OG1 A:THR238 4.7 18.8 1.0 C A:ASP239 4.8 18.1 1.0 HG1 A:THR238 4.8 22.6 1.0 C A:SER139 4.9 38.8 0.5 N A:ASP239 4.9 13.0 1.0 C A:SER139 4.9 38.8 0.5

Magnesium binding site 2 out of 2 in the X-Ray Structure of Lfa-1 I Domain in Complex with Bms-68852 Collected at 273 K


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of X-Ray Structure of Lfa-1 I Domain in Complex with Bms-68852 Collected at 273 K within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg401 b:37.9 occ:1.00 OD2 C:ASP137 2.5 26.6 0.5 HG3 C:MET140 2.5 52.2 1.0 OG C:SER139 2.5 20.3 1.0 OG1 C:THR206 2.5 15.8 1.0 HG1 C:THR206 2.6 19.0 1.0 OD1 C:ASP239 2.6 12.2 1.0 HG C:SER139 2.7 24.3 1.0 H C:SER139 3.2 11.7 1.0 H C:MET140 3.2 18.4 1.0 CG C:ASP137 3.2 20.6 0.5 HG23 C:THR206 3.3 16.6 1.0 OD1 C:ASP137 3.3 20.4 0.5 CG C:MET140 3.4 43.5 1.0 OD2 C:ASP137 3.5 11.1 0.5 CB C:THR206 3.6 11.0 1.0 OD1 C:ASP137 3.7 19.7 0.5 CG C:ASP239 3.7 10.2 1.0 N C:MET140 3.7 15.3 1.0 HB2 C:MET140 3.7 23.0 1.0 CB C:SER139 3.7 20.8 1.0 CG C:ASP137 3.7 17.1 0.5 HG21 C:THR206 3.7 16.6 1.0 CG2 C:THR206 3.7 13.9 1.0 HG2 C:MET140 3.8 52.2 1.0 N C:SER139 3.8 9.8 1.0 O C:HOH595 3.8 41.9 1.0 O C:LEU205 3.8 14.1 1.0 OD2 C:ASP239 4.0 14.0 1.0 HB3 C:SER139 4.0 24.9 1.0 CB C:MET140 4.0 19.2 1.0 CA C:SER139 4.1 11.7 1.0 HA C:THR206 4.1 11.8 1.0 HA3 C:GLY240 4.1 15.1 1.0 C C:SER139 4.1 16.1 1.0 H C:ASP239 4.2 8.7 1.0 CA C:THR206 4.3 9.8 1.0 HB C:THR206 4.4 13.2 1.0 HB2 C:SER139 4.4 24.9 1.0 C C:LEU205 4.4 12.9 1.0 N C:GLY240 4.5 9.5 1.0 HB3 C:ASP137 4.5 11.9 0.5 H C:GLY240 4.5 11.4 1.0 CA C:MET140 4.5 17.3 1.0 HE2 C:MET140 4.5 65.2 1.0 O C:HOH531 4.5 21.5 1.0 SD C:MET140 4.6 56.1 1.0 CB C:ASP137 4.6 9.7 0.5 C C:ASP239 4.7 14.5 1.0 HG22 C:THR206 4.7 16.6 1.0 N C:THR206 4.7 10.1 1.0 CB C:ASP137 4.7 9.9 0.5 HB3 C:ASP137 4.7 11.6 0.5 CA C:GLY240 4.8 12.7 1.0 O C:LEU204 4.8 21.5 1.0 C C:GLY138 4.8 17.8 1.0 HB3 C:MET140 4.9 23.0 1.0 N C:ASP239 4.9 7.3 1.0 CB C:ASP239 4.9 7.2 1.0 O C:ASP137 5.0 13.4 0.5

R.A.Woldeyes, K.K.Hallenbeck, S.J.Pfaff, G.Lee, S.V.Cortez, M.J.Kelly, K.Akassoglou, M.R.Arkin, J.S.Fraser. Divergent Conformational Dynamics Controls Allosteric Ligand Accessibility Across Evolutionarily Related I-Domain-Containing Integrins To Be Published.