Magnesium in PDB 3f74: Crystal Structure of Wild Type LFA1 I Domain

The structure of Crystal Structure of Wild Type LFA1 I Domain, PDB code: 3f74 was solved by H.Zhang, J.-H.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	61.806, 85.603, 63.554, 90.00, 117.93, 90.00
R / Rfree (%)	14.6 / 17.8

The binding sites of Magnesium atom in the Crystal Structure of Wild Type LFA1 I Domain (pdb code 3f74). 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 Wild Type LFA1 I Domain, PDB code: 3f74:

Magnesium binding site 1 out of 1 in the Crystal Structure of Wild Type LFA1 I Domain


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 Wild Type LFA1 I Domain within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg1 b:39.3 occ:1.00 OG C:SER141 1.8 17.0 1.0 O C:HOH595 2.0 12.2 1.0 OD1 C:ASP239 2.1 21.4 1.0 OG C:SER139 2.2 11.6 1.0 CG C:ASP239 3.0 17.4 1.0 CB C:SER141 3.1 14.5 1.0 OD2 C:ASP239 3.2 19.8 1.0 CB C:SER139 3.3 10.3 1.0 OG1 C:THR206 3.9 14.5 1.0 OD2 C:ASP137 4.0 14.5 1.0 N C:SER141 4.1 12.5 1.0 CA C:SER141 4.1 13.8 1.0 C C:ASP239 4.1 14.4 1.0 OD1 C:ASP137 4.2 15.2 1.0 N C:GLY240 4.2 14.0 1.0 O C:ASP239 4.3 14.1 1.0 CB C:ASP239 4.3 15.6 1.0 CG C:ASP137 4.5 14.1 1.0 CA C:GLY240 4.5 14.9 1.0 CA C:SER139 4.6 8.4 1.0 C C:SER141 4.6 13.4 1.0 O C:HOH108 4.6 18.3 1.0 N C:LEU142 4.6 12.2 1.0 CA C:ASP239 4.7 14.3 1.0 O C:HOH512 4.7 25.7 1.0 C C:SER139 4.8 9.4 1.0 N C:ASP239 4.9 13.7 1.0 CD2 C:HIS264 4.9 18.6 1.0 CG C:LEU142 5.0 14.8 1.0 O C:SER139 5.0 9.0 1.0

H.Zhang, N.S.Astrof, J.H.Liu, J.H.Wang, M.Shimaoka. Crystal Structure of Isoflurane Bound to Integrin Lfa-1 Supports A Unified Mechanism of Volatile Anesthetic Action in the Immune and Central Nervous Systems. Faseb J. V. 23 2735 2009.
ISSN: ISSN 0892-6638
PubMed: 19332643
DOI: 10.1096/FJ.09-129908