Magnesium in PDB 1qcy: The Crystal Structure of the I-Domain of Human Integrin ALPHA1BETA1

The structure of The Crystal Structure of the I-Domain of Human Integrin ALPHA1BETA1, PDB code: 1qcy was solved by J.A.Kankare, T.A.Salminen, Y.Nymalm, J.Kaepylae, J.Heino, M.S.Johnson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	500.00 / 2.30
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	74.457, 81.858, 37.316, 90.00, 90.78, 90.00
R / Rfree (%)	20 / 25.8

The binding sites of Magnesium atom in the The Crystal Structure of the I-Domain of Human Integrin ALPHA1BETA1 (pdb code 1qcy). 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 The Crystal Structure of the I-Domain of Human Integrin ALPHA1BETA1, PDB code: 1qcy:

Magnesium binding site 1 out of 1 in the The Crystal Structure of the I-Domain of Human Integrin ALPHA1BETA1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Crystal Structure of the I-Domain of Human Integrin ALPHA1BETA1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg101 b:39.9 occ:1.00 OG A:SER154 2.4 20.0 1.0 O A:HOH5 2.4 16.1 1.0 O A:HOH48 2.5 30.4 1.0 O A:HOH47 2.6 14.5 1.0 OD1 A:ASP253 2.6 14.4 1.0 OG A:SER152 2.8 28.1 1.0 CB A:SER152 3.3 19.8 1.0 CG A:ASP253 3.5 16.4 1.0 CB A:SER154 3.6 15.5 1.0 OD2 A:ASP253 3.7 15.3 1.0 OG1 A:THR220 4.0 31.3 1.0 O A:ASP253 4.2 18.8 1.0 OD2 A:ASP150 4.4 20.2 1.0 C A:ASP253 4.4 19.3 1.0 N A:GLY254 4.6 21.7 1.0 CA A:GLY254 4.6 22.1 1.0 N A:SER154 4.6 17.8 1.0 CA A:SER154 4.7 17.5 1.0 CA A:SER152 4.7 20.1 1.0 OG A:SER284 4.8 20.0 1.0 CB A:ASP253 4.9 15.0 1.0

Y.Nymalm, J.S.Puranen, T.K.M.Nyholm, J.Kaepylae, H.Kidron, O.T.Pentikaeinen, T.T.Airenne, J.Heino, J.P.Slotte, M.S.Johnson, T.A.Salminen. Jararhagin-Derived Rkkh Peptides Induce Structural Changes in A1I Domain of Human Integrin A1B1 J.Biol.Chem. V. 279 7962 2004.
ISSN: ISSN 0021-9258
PubMed: 14660600
DOI: 10.1074/JBC.M312912200