Magnesium in PDB 3q7e: Crystal Structure of Rat Protein Arginine Methyltransferase 1 (PRMT1) M48L Mutant

The structure of Crystal Structure of Rat Protein Arginine Methyltransferase 1 (PRMT1) M48L Mutant, PDB code: 3q7e was solved by S.J.Johnson, P.J.Porter, J.M.Hevel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.69 / 2.20
Space group	P 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	87.307, 87.307, 143.290, 90.00, 90.00, 90.00
R / Rfree (%)	20.1 / 24.5

The binding sites of Magnesium atom in the Crystal Structure of Rat Protein Arginine Methyltransferase 1 (PRMT1) M48L Mutant (pdb code 3q7e). 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 Rat Protein Arginine Methyltransferase 1 (PRMT1) M48L Mutant, PDB code: 3q7e:

Magnesium binding site 1 out of 1 in the Crystal Structure of Rat Protein Arginine Methyltransferase 1 (PRMT1) M48L Mutant


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 Rat Protein Arginine Methyltransferase 1 (PRMT1) M48L Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg354 b:61.8 occ:1.00 ND2 A:ASN60 2.7 35.7 1.0 NE A:ARG59 2.9 30.6 1.0 N A:ASN60 3.3 29.0 1.0 C A:ARG59 3.4 31.4 1.0 CB A:PHE63 3.4 31.4 1.0 O A:ARG59 3.4 37.6 1.0 CG A:ARG59 3.5 34.5 1.0 CA A:ASN60 3.5 30.7 1.0 CD2 A:PHE63 3.6 33.5 1.0 O A:HOH528 3.6 38.7 1.0 CB A:ARG59 3.7 27.6 1.0 CG A:PHE63 3.7 33.1 1.0 NH2 A:ARG59 3.7 22.9 1.0 CD A:ARG59 3.7 32.3 1.0 CZ A:ARG59 3.7 34.4 1.0 CG A:ASN60 3.8 37.4 1.0 CA A:ARG59 4.1 26.9 1.0 NE2 A:HIS64 4.2 48.3 1.0 CB A:ASN60 4.3 30.9 1.0 O A:HOH405 4.5 54.4 1.0 CE2 A:PHE63 4.6 30.8 1.0 CE1 A:HIS64 4.6 53.3 1.0 O A:LEU56 4.7 36.5 1.0 C A:ASN60 4.7 29.5 1.0 CA A:PHE63 4.7 32.0 1.0 CD2 A:HIS64 4.7 51.6 1.0 CD1 A:PHE63 4.7 32.6 1.0 OD1 A:ASN60 4.9 44.8 1.0 N A:PHE63 4.9 34.8 1.0 NH1 A:ARG59 5.0 29.9 1.0

S.Gui, W.L.Wooderchak, M.P.Daly, P.J.Porter, S.J.Johnson, J.M.Hevel. Investigation of the Molecular Origins of Protein-Arginine Methyltransferase I (PRMT1) Product Specificity Reveals A Role For Two Conserved Methionine Residues. J.Biol.Chem. V. 286 29118 2011.
ISSN: ISSN 0021-9258
PubMed: 21697082
DOI: 10.1074/JBC.M111.224097