Magnesium in PDB 7kc3: X-Ray Structure of Lfa-1 I Domain Collected at 273 K

The structure of X-Ray Structure of Lfa-1 I Domain Collected at 273 K, PDB code: 7kc3 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)	45.42 / 1.80
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	104.896, 104.896, 51.644, 90, 90, 120
R / Rfree (%)	17.4 / 21.2

The binding sites of Magnesium atom in the X-Ray Structure of Lfa-1 I Domain Collected at 273 K (pdb code 7kc3). 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 X-Ray Structure of Lfa-1 I Domain Collected at 273 K, PDB code: 7kc3:

Magnesium binding site 1 out of 1 in the X-Ray Structure of Lfa-1 I Domain 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 Collected at 273 K within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg401 b:20.2 occ:1.00 OD1 C:ASP239 2.0 18.7 1.0 O C:HOH538 2.1 21.5 1.0 O C:HOH544 2.1 18.2 1.0 OG C:SER139 2.1 18.2 1.0 OG C:SER141 2.1 19.2 1.0 CG C:ASP239 3.0 21.6 1.0 HB2 C:SER139 3.2 21.2 1.0 CB C:SER139 3.2 17.7 1.0 HB3 C:SER141 3.2 24.0 1.0 CB C:SER141 3.2 20.0 1.0 OD2 C:ASP239 3.3 20.9 1.0 H C:SER141 3.4 22.7 1.0 HG1 C:THR206 3.5 22.6 1.0 HA3 C:GLY240 3.5 26.9 1.0 HB3 C:SER139 3.5 21.2 1.0 HB2 C:SER141 3.8 24.0 1.0 O C:ASP239 3.9 20.8 1.0 C C:ASP239 3.9 20.9 1.0 OD2 C:ASP137 4.0 18.0 1.0 OG1 C:THR206 4.0 18.8 1.0 OD1 C:ASP137 4.1 20.0 1.0 N C:GLY240 4.1 19.4 1.0 N C:SER141 4.2 18.9 1.0 HG C:LEU142 4.2 26.1 1.0 H C:ASP239 4.2 22.1 1.0 CA C:GLY240 4.2 22.4 1.0 CB C:ASP239 4.3 20.2 1.0 CA C:SER141 4.3 18.9 1.0 CG C:ASP137 4.4 21.1 1.0 CA C:SER139 4.5 19.0 1.0 H C:GLY240 4.5 23.2 1.0 O C:HOH514 4.5 31.9 1.0 CA C:ASP239 4.6 17.6 1.0 H C:LEU142 4.6 23.9 1.0 C C:SER139 4.7 18.1 1.0 HA2 C:GLY240 4.7 26.9 1.0 H C:SER139 4.7 18.8 1.0 N C:ASP239 4.8 18.4 1.0 HB2 C:ASP239 4.8 24.2 1.0 HB3 C:ASP239 4.9 24.2 1.0 H C:MET140 4.9 21.3 1.0 HG21 C:THR206 4.9 19.6 1.0 O C:HOH556 4.9 29.1 1.0 N C:MET140 4.9 17.8 1.0 N C:LEU142 5.0 19.9 1.0 C C:SER141 5.0 21.6 1.0

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.