Ruthenium in PDB 3we8: Pim-1 Kinase in Complex with Ruthenium-Based Inhibitor

All present enzymatic activity of Pim-1 Kinase in Complex with Ruthenium-Based Inhibitor:
2.7.11.1;

The structure of Pim-1 Kinase in Complex with Ruthenium-Based Inhibitor, PDB code: 3we8 was solved by K.Waehler, K.Kraeling, H.Steuber, E.Meggers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.32 / 1.95
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	97.730, 97.730, 81.190, 90.00, 90.00, 120.00
R / Rfree (%)	15.1 / 17.7

The binding sites of Ruthenium atom in the Pim-1 Kinase in Complex with Ruthenium-Based Inhibitor (pdb code 3we8). This binding sites where shown within 5.0 Angstroms radius around Ruthenium atom.
In total only one binding site of Ruthenium was determined in the Pim-1 Kinase in Complex with Ruthenium-Based Inhibitor, PDB code: 3we8:

Ruthenium binding site 1 out of 1 in the Pim-1 Kinase in Complex with Ruthenium-Based Inhibitor


Mono view


Stereo pair view

A full contact list of Ruthenium with other atoms in the Ru binding site number 1 of Pim-1 Kinase in Complex with Ruthenium-Based Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Ru401 b:26.0 occ:1.00 RU A:RUI401 0.0 26.0 1.0 C13 A:RUI401 1.3 27.5 1.0 C3 A:RUI401 2.1 22.4 1.0 N1 A:RUI401 2.2 24.5 1.0 C18 A:RUI401 2.2 30.8 1.0 C16 A:RUI401 2.2 25.8 1.0 C17 A:RUI401 2.2 26.3 1.0 C15 A:RUI401 2.2 31.8 1.0 C14 A:RUI401 2.2 33.0 1.0 O11 A:RUI401 2.6 24.2 1.0 C7 A:RUI401 3.0 25.9 1.0 C1 A:RUI401 3.0 22.6 1.0 C9 A:RUI401 3.1 26.4 1.0 C4 A:RUI401 3.2 23.3 1.0 C8 A:RUI401 4.3 28.4 1.0 C A:RUI401 4.3 24.2 1.0 C11 A:RUI401 4.4 31.3 1.0 N A:RUI401 4.4 22.2 1.0 CD1 A:ILE185 4.7 13.1 1.0 CZ A:PHE49 4.8 23.9 1.0 CD2 A:LEU174 4.9 20.3 1.0 C10 A:RUI401 4.9 31.6 1.0 C2 A:RUI401 4.9 24.6 1.0 CE2 A:PHE49 5.0 27.0 1.0

K.Wahler, K.Kraling, H.Steuber, E.Meggers. Non-Atp-Mimetic Organometallic Protein Kinase Inhibitor Chemistryopen V. 2 180 2013.
ISSN: ESSN 2191-1363
PubMed: 24551564
DOI: 10.1002/OPEN.201300031