Magnesium in PDB 4kit: Crystal Structure of Human BRR2 in Complex with the PRP8 JAB1/Mpn Domain

All present enzymatic activity of Crystal Structure of Human BRR2 in Complex with the PRP8 JAB1/Mpn Domain:
3.6.4.13;

The structure of Crystal Structure of Human BRR2 in Complex with the PRP8 JAB1/Mpn Domain, PDB code: 4kit was solved by M.C.Wahl, T.Wandersleben, K.F.Santos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.20 / 3.60
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	240.002, 240.002, 201.089, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 23.5

The binding sites of Magnesium atom in the Crystal Structure of Human BRR2 in Complex with the PRP8 JAB1/Mpn Domain (pdb code 4kit). 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 Human BRR2 in Complex with the PRP8 JAB1/Mpn Domain, PDB code: 4kit:

Magnesium binding site 1 out of 1 in the Crystal Structure of Human BRR2 in Complex with the PRP8 JAB1/Mpn 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 Human BRR2 in Complex with the PRP8 JAB1/Mpn Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg2203 b:0.1 occ:1.00 O2B B:ADP2202 1.9 0.6 1.0 O3B B:ADP2202 2.5 0.5 1.0 PB B:ADP2202 2.6 0.6 1.0 OD2 B:ASP1454 2.7 0.2 1.0 O3A B:ADP2202 3.5 0.4 1.0 CG2 B:THR1357 3.5 0.2 1.0 CG B:ASP1454 3.8 0.4 1.0 OE2 B:GLU1455 3.8 0.5 1.0 OE1 B:GLU1455 3.9 0.6 1.0 O1B B:ADP2202 3.9 0.1 1.0 CD2 B:LEU1385 4.0 0.9 1.0 OD1 B:ASP1454 4.2 0.0 1.0 CD B:GLU1455 4.2 0.5 1.0 OH B:TYR1378 4.8 0.4 1.0 PA B:ADP2202 4.8 0.2 1.0 CD1 B:LEU1385 4.9 0.6 1.0 CG B:LEU1385 5.0 0.9 1.0 CB B:THR1357 5.0 0.9 1.0

S.Mozaffari-Jovin, T.Wandersleben, K.F.Santos, C.L.Will, R.Luhrmann, M.C.Wahl. Inhibition of Rna Helicase BRR2 By the C-Terminal Tail of the Spliceosomal Protein PRP8. Science V. 341 80 2013.
ISSN: ISSN 0036-8075
PubMed: 23704370
DOI: 10.1126/SCIENCE.1237515