Magnesium in PDB 2oy3: Crystal Structure Analysis of the Monomeric Srcr Domain of Mouse Marco

The structure of Crystal Structure Analysis of the Monomeric Srcr Domain of Mouse Marco, PDB code: 2oy3 was solved by J.R.M.Ojala, T.Pikkarainen, A.Tuuttila, T.Sandalova, K.Tryggvason, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.70 / 1.78
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	32.345, 28.060, 42.665, 90.00, 99.19, 90.00
R / Rfree (%)	16.1 / 21

The binding sites of Magnesium atom in the Crystal Structure Analysis of the Monomeric Srcr Domain of Mouse Marco (pdb code 2oy3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure Analysis of the Monomeric Srcr Domain of Mouse Marco, PDB code: 2oy3:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure Analysis of the Monomeric Srcr Domain of Mouse Marco


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure Analysis of the Monomeric Srcr Domain of Mouse Marco within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg201 b:28.3 occ:1.00 O A:HOH21 2.0 20.8 1.0 OD1 A:ASP448 2.2 23.8 1.0 O A:HOH24 2.2 25.9 1.0 O A:HOH16 2.2 18.3 1.0 O A:HOH31 2.2 28.3 1.0 O A:HOH7 2.3 19.0 1.0 CG A:ASP448 3.2 21.6 1.0 OD2 A:ASP448 3.5 24.6 1.0 OE1 A:GLU511 4.0 16.8 1.0 CD A:GLU511 4.0 15.3 1.0 OE2 A:GLU511 4.1 18.8 1.0 OD1 A:ASP447 4.5 17.2 1.0 CB A:ASP448 4.6 17.0 1.0 CG A:GLU511 4.8 13.8 1.0 OD1 A:ASN506 4.9 24.9 0.5 CA A:ASP448 5.0 17.4 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure Analysis of the Monomeric Srcr Domain of Mouse Marco


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure Analysis of the Monomeric Srcr Domain of Mouse Marco within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg202 b:32.2 occ:1.00 O A:HOH53 2.1 27.1 1.0 O A:ASP449 2.2 19.1 1.0 O A:VAL485 2.3 19.6 1.0 O A:HOH15 2.4 18.5 1.0 OD2 A:ASP454 2.5 20.6 1.0 CG A:ASP454 3.3 17.6 1.0 C A:ASP449 3.4 17.7 1.0 C A:VAL485 3.4 19.8 1.0 OD1 A:ASP454 3.5 19.2 1.0 OD2 A:ASP451 3.7 18.0 1.0 CA A:ASN486 3.8 23.5 1.0 CG A:ASP451 3.8 20.4 1.0 N A:ASN486 4.0 21.8 1.0 OD1 A:ASP451 4.0 25.7 1.0 N A:ASP451 4.0 16.6 1.0 OD1 A:ASN486 4.1 30.6 1.0 CB A:ASP449 4.1 18.4 1.0 N A:TRP450 4.2 16.4 1.0 CA A:TRP450 4.3 15.6 1.0 CA A:ASP449 4.4 17.7 1.0 C A:TRP450 4.5 16.1 1.0 CB A:ASP451 4.6 18.0 1.0 CA A:VAL485 4.6 19.0 1.0 CB A:ASN486 4.7 23.9 1.0 C A:ASN486 4.7 23.8 1.0 N A:CYS487 4.7 23.9 1.0 CG A:ASN486 4.8 27.5 1.0 CB A:ASP454 4.8 14.9 1.0 N A:VAL485 4.9 19.4 1.0 CA A:ASP451 4.9 17.2 1.0

J.R.Ojala, T.Pikkarainen, A.Tuuttila, T.Sandalova, K.Tryggvason. Crystal Structure of the Cysteine-Rich Domain of Scavenger Receptor Marco Reveals the Presence of A Basic and An Acidic Cluster That Both Contribute to Ligand Recognition. J.Biol.Chem. V. 282 16654 2007.
ISSN: ISSN 0021-9258
PubMed: 17405873
DOI: 10.1074/JBC.M701750200