Magnesium in PDB 4yzm: Humanized ROCO4 Bound to LRRK2-IN1

All present enzymatic activity of Humanized ROCO4 Bound to LRRK2-IN1:
2.7.11.1;

The structure of Humanized ROCO4 Bound to LRRK2-IN1, PDB code: 4yzm was solved by B.K.Gilsbach, A.C.Messias, G.Ito, M.Sattler, D.R.Alessi, A.Wittinghofer, A.Kortholt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.43 / 3.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	43.030, 89.070, 177.710, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 28.2

The binding sites of Magnesium atom in the Humanized ROCO4 Bound to LRRK2-IN1 (pdb code 4yzm). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Humanized ROCO4 Bound to LRRK2-IN1, PDB code: 4yzm:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Humanized ROCO4 Bound to LRRK2-IN1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Humanized ROCO4 Bound to LRRK2-IN1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1302 b:26.5 occ:1.00 OD2 A:ASP1154 1.6 38.5 1.0 OD1 A:ASP1177 2.5 45.5 1.0 CG A:ASP1154 2.8 36.1 1.0 CB A:ASP1154 3.5 34.7 1.0 CG A:ASP1177 3.5 42.6 1.0 O A:SER1181 3.7 60.9 1.0 OD1 A:ASP1154 3.8 34.3 1.0 OD2 A:ASP1177 4.0 43.8 1.0 OE2 A:GLU1074 4.0 46.8 1.0 O A:GLY1179 4.1 61.4 1.0 OG A:SER1181 4.1 57.0 1.0 O A:ASP1177 4.1 36.3 1.0 NH2 A:ARG1156 4.5 29.4 1.0 CA A:GLY1036 4.5 43.6 1.0 C A:SER1181 4.7 57.3 1.0 CB A:ASP1177 4.7 41.1 1.0 CA A:ASP1154 5.0 31.5 1.0 N A:SER1181 5.0 54.5 1.0

Magnesium binding site 2 out of 2 in the Humanized ROCO4 Bound to LRRK2-IN1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Humanized ROCO4 Bound to LRRK2-IN1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1302 b:33.0 occ:1.00 OD2 B:ASP1177 1.4 46.0 1.0 OD2 B:ASP1154 2.3 35.1 1.0 CG B:ASP1177 2.6 44.1 1.0 O B:LEU1191 3.2 83.6 1.0 OD1 B:ASP1177 3.3 48.8 1.0 CG B:ASP1154 3.4 33.6 1.0 O B:SER1181 3.8 42.6 1.0 CB B:ASP1154 3.8 32.4 1.0 CB B:ASP1177 3.9 38.4 1.0 C B:LEU1191 4.0 89.8 1.0 CA B:LEU1191 4.0 85.4 1.0 O B:GLY1179 4.1 55.0 1.0 OE2 B:GLU1074 4.1 43.2 1.0 OG B:SER1181 4.4 36.7 1.0 O B:GLY1036 4.4 54.7 1.0 OD1 B:ASP1154 4.5 31.9 1.0 N B:LEU1191 4.7 84.1 1.0 C B:SER1181 4.8 43.8 1.0 C B:GLY1036 4.9 51.9 1.0

B.K.Gilsbach, A.C.Messias, G.Ito, M.Sattler, D.R.Alessi, A.Wittinghofer, A.Kortholt. Structural Characterization of LRRK2 Inhibitors. J.Med.Chem. V. 58 3751 2015.
ISSN: ISSN 0022-2623
PubMed: 25897865
DOI: 10.1021/JM5018779