Magnesium in PDB 4f93: BRR2 Helicase Region S1087L, Mg-Atp

All present enzymatic activity of BRR2 Helicase Region S1087L, Mg-Atp:
3.6.4.13;

The structure of BRR2 Helicase Region S1087L, Mg-Atp, PDB code: 4f93 was solved by K.F.Santos, S.M.Jovin, G.Weber, V.Pena, R.Luehrmann, M.C.Wahl, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.36 / 2.92
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	147.120, 154.586, 143.280, 90.00, 120.62, 90.00
R / Rfree (%)	19.7 / 24.8

The binding sites of Magnesium atom in the BRR2 Helicase Region S1087L, Mg-Atp (pdb code 4f93). 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 BRR2 Helicase Region S1087L, Mg-Atp, PDB code: 4f93:

Magnesium binding site 1 out of 1 in the BRR2 Helicase Region S1087L, Mg-Atp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of BRR2 Helicase Region S1087L, Mg-Atp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg3003 b:0.6 occ:1.00 O1G B:ATP3002 2.6 0.8 1.0 O1B B:ATP3002 3.0 0.7 1.0 OD1 B:ASP1454 3.0 0.8 1.0 O3G B:ATP3002 3.0 0.0 1.0 OD2 B:ASP1454 3.1 0.6 1.0 PG B:ATP3002 3.1 0.6 1.0 O B:HOH3121 3.3 0.4 1.0 O3B B:ATP3002 3.4 0.1 1.0 CG B:ASP1454 3.4 0.3 1.0 PB B:ATP3002 3.8 0.6 1.0 CE B:LYS1356 4.0 90.1 1.0 CB B:LYS1356 4.1 94.6 1.0 OG1 B:THR1357 4.2 0.7 1.0 OE2 B:GLU1455 4.2 0.2 1.0 N B:THR1357 4.3 83.0 1.0 CD1 B:LEU1490 4.6 0.9 1.0 O2G B:ATP3002 4.6 0.4 1.0 CD B:GLU1455 4.6 0.9 1.0 C B:LYS1356 4.7 0.9 1.0 NZ B:LYS1356 4.7 87.3 1.0 CA B:THR1357 4.8 99.0 1.0 CB B:LEU1490 4.8 93.1 1.0 O B:HOH3113 4.8 83.6 1.0 CA B:LYS1356 4.9 0.1 1.0 O3A B:ATP3002 4.9 0.8 1.0 CB B:ASP1454 4.9 93.0 1.0 CG B:GLU1455 4.9 98.9 1.0 CG B:LYS1356 4.9 89.0 1.0 O2B B:ATP3002 4.9 96.5 1.0 CD B:LYS1356 5.0 93.7 1.0 CB B:THR1357 5.0 98.2 1.0

K.F.Santos, S.M.Jovin, G.Weber, V.Pena, R.Luhrmann, M.C.Wahl. Structural Basis For Functional Cooperation Between Tandem Helicase Cassettes in BRR2-Mediated Remodeling of the Spliceosome. Proc.Natl.Acad.Sci.Usa V. 109 17418 2012.
ISSN: ISSN 0027-8424
PubMed: 23045696
DOI: 10.1073/PNAS.1208098109