Magnesium in PDB 4f1m: Crystal Structure of the G1179S ROCO4 Kinase Domain Bound to Appcp From D. Discoideum.

All present enzymatic activity of Crystal Structure of the G1179S ROCO4 Kinase Domain Bound to Appcp From D. Discoideum.:
2.7.11.1;

The structure of Crystal Structure of the G1179S ROCO4 Kinase Domain Bound to Appcp From D. Discoideum., PDB code: 4f1m was solved by B.K.Gilsbach, I.R.Vetter, A.Wittinghofer, A.Kortholt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.95 / 2.04
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	42.283, 42.283, 332.847, 90.00, 90.00, 90.00
R / Rfree (%)	26.1 / 29.4

The binding sites of Magnesium atom in the Crystal Structure of the G1179S ROCO4 Kinase Domain Bound to Appcp From D. Discoideum. (pdb code 4f1m). 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 the G1179S ROCO4 Kinase Domain Bound to Appcp From D. Discoideum., PDB code: 4f1m:

Magnesium binding site 1 out of 1 in the Crystal Structure of the G1179S ROCO4 Kinase Domain Bound to Appcp From D. Discoideum.


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 the G1179S ROCO4 Kinase Domain Bound to Appcp From D. Discoideum. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1303 b:30.0 occ:1.00 OD2 A:ASP1154 2.5 30.4 1.0 OD1 A:ASP1177 3.0 42.3 1.0 O A:SER1179 3.2 48.8 1.0 CG A:ASP1154 3.4 30.0 1.0 O A:ASP1177 3.5 38.5 1.0 CB A:ASP1154 3.6 29.9 1.0 CG A:ASP1177 3.6 41.0 1.0 O A:HOH1481 3.7 41.4 1.0 CG A:LEU1180 3.9 48.7 1.0 C A:SER1179 4.0 47.7 1.0 CB A:ASP1177 4.0 39.6 1.0 ND2 A:ASN1159 4.1 23.6 1.0 O2G A:ACP1301 4.2 64.8 1.0 C A:ASP1177 4.2 38.7 1.0 N A:SER1179 4.3 45.2 1.0 CB A:LEU1180 4.3 48.8 1.0 OD2 A:ASP1177 4.4 41.6 1.0 CA A:SER1179 4.5 46.8 1.0 OD1 A:ASP1154 4.5 30.2 1.0 CD1 A:LEU1180 4.6 48.3 1.0 CA A:ASP1177 4.7 38.5 1.0 CB A:SER1179 4.8 47.9 1.0 CD2 A:LEU1180 4.9 49.2 1.0 CG A:ASN1159 4.9 24.0 1.0 N A:LEU1180 5.0 48.2 1.0

B.K.Gilsbach, F.Y.Ho, I.R.Vetter, P.J.Van Haastert, A.Wittinghofer, A.Kortholt. Roco Kinase Structures Give Insights Into the Mechanism of Parkinson Disease-Related Leucine-Rich-Repeat Kinase 2 Mutations. Proc.Natl.Acad.Sci.Usa V. 109 10322 2012.
ISSN: ISSN 0027-8424
PubMed: 22689969
DOI: 10.1073/PNAS.1203223109