Magnesium in PDB 4jke: Open and Closed Forms of T1789P Human PRP8 Rnase H-Like Domain with Bound Mg Ion

The structure of Open and Closed Forms of T1789P Human PRP8 Rnase H-Like Domain with Bound Mg Ion, PDB code: 4jke was solved by M.J.Schellenberg, T.Wu, D.B.Ritchie, K.A.Atta, A.M.Macmillan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.26 / 1.65
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	76.181, 77.077, 93.042, 90.00, 90.00, 90.00
R / Rfree (%)	15.6 / 20.3

The binding sites of Magnesium atom in the Open and Closed Forms of T1789P Human PRP8 Rnase H-Like Domain with Bound Mg Ion (pdb code 4jke). 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 Open and Closed Forms of T1789P Human PRP8 Rnase H-Like Domain with Bound Mg Ion, PDB code: 4jke:

Magnesium binding site 1 out of 1 in the Open and Closed Forms of T1789P Human PRP8 Rnase H-Like Domain with Bound Mg Ion


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Open and Closed Forms of T1789P Human PRP8 Rnase H-Like Domain with Bound Mg Ion within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg2001 b:26.3 occ:0.50 O B:HOH2273 1.8 27.9 0.5 O B:HOH2270 1.9 22.2 0.5 OD1 B:ASP1781 2.2 25.4 1.0 O B:HOH2156 2.2 19.3 0.5 O B:HOH2271 2.9 39.6 1.0 CG B:ASP1781 3.0 23.3 1.0 OD2 B:ASP1781 3.1 28.0 1.0 OE1 B:GLN1894 4.1 31.3 1.0 OG1 B:THR1864 4.2 34.9 1.0 O B:ASP1782 4.2 20.1 1.0 CB B:ASP1781 4.4 20.4 1.0 O B:HOH2190 4.4 34.2 1.0 O B:HOH2246 4.6 20.6 0.5 O B:HOH2140 4.6 24.7 1.0 N B:ASP1782 4.8 17.4 1.0 OD1 B:ASP1782 4.8 27.1 0.6 CD B:GLN1894 4.9 32.3 1.0 NE2 B:GLN1894 4.9 39.3 1.0 O B:HOH2146 4.9 34.7 1.0 CA B:ASP1781 5.0 18.0 1.0

M.J.Schellenberg, T.Wu, D.B.Ritchie, S.Fica, J.P.Staley, K.A.Atta, P.Lapointe, A.M.Macmillan. A Conformational Switch in PRP8 Mediates Metal Ion Coordination That Promotes Pre-Mrna Exon Ligation. Nat.Struct.Mol.Biol. V. 20 728 2013.
ISSN: ISSN 1545-9993
PubMed: 23686287
DOI: 10.1038/NSMB.2556