Ruthenium in PDB 2cfk: Agao in Complex with WC5 (Ru-Wire Inhibitor, 5-Carbon Linker)

All present enzymatic activity of Agao in Complex with WC5 (Ru-Wire Inhibitor, 5-Carbon Linker):
1.4.3.6;

The structure of Agao in Complex with WC5 (Ru-Wire Inhibitor, 5-Carbon Linker), PDB code: 2cfk was solved by D.B.Langley, A.P.Duff, H.C.Freeman, J.M.Guss, G.A.Juda, D.M.Dooley, S.M.Contakes, N.W.Halpern-Manners, A.R.Dunn, H.B.Gray, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.02 / 1.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	157.885, 62.944, 92.013, 90.00, 112.20, 90.00
R / Rfree (%)	14.5 / 16.5

The structure of Agao in Complex with WC5 (Ru-Wire Inhibitor, 5-Carbon Linker) also contains other interesting chemical elements:

Copper	(Cu)	1 atom
Sodium	(Na)	1 atom

The binding sites of Ruthenium atom in the Agao in Complex with WC5 (Ru-Wire Inhibitor, 5-Carbon Linker) (pdb code 2cfk). This binding sites where shown within 5.0 Angstroms radius around Ruthenium atom.
In total 2 binding sites of Ruthenium where determined in the Agao in Complex with WC5 (Ru-Wire Inhibitor, 5-Carbon Linker), PDB code: 2cfk:
Jump to Ruthenium binding site number: 1; 2;

Ruthenium binding site 1 out of 2 in the Agao in Complex with WC5 (Ru-Wire Inhibitor, 5-Carbon Linker)


Mono view


Stereo pair view

A full contact list of Ruthenium with other atoms in the Ru binding site number 1 of Agao in Complex with WC5 (Ru-Wire Inhibitor, 5-Carbon Linker) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ru1631 b:40.1 occ:0.20 RU A:R5A1631 0.0 40.1 0.2 NAA A:R5A1631 2.1 46.1 0.2 NBL A:R5A1631 2.1 48.5 0.2 NAD A:R5A1631 2.1 44.5 0.2 NCL A:R5A1631 2.1 46.5 0.2 NBA A:R5A1631 2.1 49.5 0.2 NCA A:R5A1631 2.1 46.1 0.2 NBA A:R5B1632 2.1 46.5 0.2 CBB A:R5B1632 2.2 44.7 0.2 NAD A:R5B1632 2.4 47.2 0.2 CAE A:R5B1632 2.4 47.5 0.2 CBF A:R5B1632 2.4 46.5 0.2 CBC A:R5B1632 2.5 43.3 0.2 HCK A:R5B1632 2.7 44.3 0.2 HAN A:R5B1632 2.8 46.7 0.2 CBE A:R5B1632 2.8 45.8 0.2 CAB A:R5A1631 2.9 46.0 0.2 CCF A:R5A1631 2.9 46.9 0.2 CBF A:R5A1631 2.9 51.7 0.2 CAC A:R5A1631 2.9 43.7 0.2 CBD A:R5B1632 2.9 45.5 0.2 CCG A:R5A1631 2.9 48.0 0.2 CAC A:R5B1632 2.9 46.8 0.2 CBG A:R5A1631 2.9 50.6 0.2 CBB A:R5A1631 2.9 52.8 0.2 CCB A:R5A1631 2.9 43.3 0.2 CAF A:R5B1632 3.0 45.8 0.2 HCK A:R5A1631 3.0 53.0 0.2 HBK A:R5A1631 3.0 45.2 0.2 CBK A:R5A1631 3.0 50.1 0.2 CAE A:R5A1631 3.1 44.1 0.2 CCK A:R5A1631 3.1 47.9 0.2 CAN A:R5A1631 3.1 47.9 0.2 HCB A:R5A1631 3.2 50.4 0.2 HAN A:R5A1631 3.2 44.1 0.2 HBB A:R5A1631 3.2 48.1 0.2 HAE A:R5A1631 3.2 47.9 0.2 HCJ A:R5B1632 3.3 43.6 0.2 RU A:R5B1632 3.4 48.4 0.2 CBG A:R5B1632 3.4 46.6 0.2 CAG A:R5B1632 3.5 46.5 0.2 CAH A:R5B1632 3.5 46.5 0.2 HAM A:R5B1632 3.6 46.0 0.2 HCH A:R5B1632 3.7 45.5 0.2 HCI A:R5B1632 3.7 44.6 0.2 CAB A:R5B1632 3.8 48.2 0.2 NBL A:R5B1632 3.8 46.0 0.2 NAA A:R5B1632 4.0 47.2 0.2 CBC A:R5A1631 4.2 54.3 0.2 CCC A:R5A1631 4.2 47.1 0.2 CCH A:R5A1631 4.3 48.3 0.2 CBH A:R5A1631 4.3 51.3 0.2 CAK A:R5A1631 4.3 47.7 0.2 CCE A:R5A1631 4.3 47.7 0.2 CBE A:R5A1631 4.3 54.0 0.2 CAH A:R5A1631 4.3 44.6 0.2 CBJ A:R5A1631 4.3 51.3 0.2 CCJ A:R5A1631 4.3 48.3 0.2 CAM A:R5A1631 4.3 47.8 0.2 CAF A:R5A1631 4.3 42.8 0.2 CBH A:R5B1632 4.4 46.1 0.2 CAI A:R5B1632 4.6 45.3 0.2 HL11 A:R5B1632 4.6 45.6 0.2 HCE A:R5B1632 4.7 45.7 0.2 CL0 A:R5B1632 4.7 45.9 0.2 HBB A:R5B1632 4.8 49.2 0.2 CBD A:R5A1631 4.8 54.4 0.2 CCD A:R5A1631 4.8 48.1 0.2 CBI A:R5A1631 4.8 52.0 0.2 CCI A:R5A1631 4.8 49.3 0.2 CA0 A:R5A1631 4.8 49.2 0.2 CAK A:R5B1632 4.9 47.7 0.2 CAG A:R5A1631 4.9 44.4 0.2 HBK A:R5B1632 5.0 47.9 0.2

Ruthenium binding site 2 out of 2 in the Agao in Complex with WC5 (Ru-Wire Inhibitor, 5-Carbon Linker)


Mono view


Stereo pair view

A full contact list of Ruthenium with other atoms in the Ru binding site number 2 of Agao in Complex with WC5 (Ru-Wire Inhibitor, 5-Carbon Linker) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ru1632 b:48.4 occ:0.20 RU A:R5B1632 0.0 48.4 0.2 HAE A:R5A1631 0.7 47.9 0.2 CAN A:R5A1631 1.5 47.9 0.2 NBL A:R5B1632 2.1 46.0 0.2 NCL A:R5B1632 2.1 48.2 0.2 NBA A:R5B1632 2.1 46.5 0.2 NAD A:R5B1632 2.1 47.2 0.2 NAA A:R5B1632 2.1 47.2 0.2 NCA A:R5B1632 2.1 47.7 0.2 NAA A:R5A1631 2.5 46.1 0.2 CAM A:R5A1631 2.5 47.8 0.2 HAF A:R5A1631 2.7 48.5 0.2 NCL A:R5A1631 2.8 46.5 0.2 CCG A:R5A1631 2.8 48.0 0.2 CBF A:R5B1632 2.9 46.5 0.2 CCF A:R5B1632 2.9 49.2 0.2 CAC A:R5B1632 2.9 46.8 0.2 CAB A:R5B1632 2.9 48.2 0.2 CBB A:R5B1632 2.9 44.7 0.2 CCB A:R5B1632 2.9 48.8 0.2 CBG A:R5B1632 2.9 46.6 0.2 CCG A:R5B1632 2.9 50.1 0.2 HCK A:R5B1632 3.0 44.3 0.2 HBK A:R5B1632 3.0 47.9 0.2 CCK A:R5B1632 3.0 49.8 0.2 CBK A:R5B1632 3.0 46.1 0.2 CAE A:R5B1632 3.1 47.5 0.2 CAN A:R5B1632 3.1 46.8 0.2 HBB A:R5B1632 3.1 49.2 0.2 HCB A:R5B1632 3.1 45.5 0.2 CCF A:R5A1631 3.2 46.9 0.2 HAN A:R5B1632 3.2 46.7 0.2 HAE A:R5B1632 3.2 46.6 0.2 CCK A:R5A1631 3.3 47.9 0.2 NCA A:R5A1631 3.4 46.1 0.2 RU A:R5A1631 3.4 40.1 0.2 CCH A:R5A1631 3.4 48.3 0.2 CAB A:R5A1631 3.7 46.0 0.2 CA0 A:R5A1631 3.8 49.2 0.2 CCJ A:R5A1631 3.9 48.3 0.2 HBB A:R5A1631 3.9 48.1 0.2 CCI A:R5A1631 3.9 49.3 0.2 HCK A:R5A1631 4.0 53.0 0.2 HBE A:R5A1631 4.0 48.9 0.2 CCE A:R5A1631 4.1 47.7 0.2 CBC A:R5B1632 4.2 43.3 0.2 CCC A:R5B1632 4.2 47.6 0.2 CBH A:R5B1632 4.3 46.1 0.2 CCH A:R5B1632 4.3 50.3 0.2 CAK A:R5A1631 4.3 47.7 0.2 CCB A:R5A1631 4.3 43.3 0.2 CBE A:R5B1632 4.3 45.8 0.2 CCE A:R5B1632 4.3 48.8 0.2 CBJ A:R5B1632 4.3 44.9 0.2 CCJ A:R5B1632 4.3 50.3 0.2 CAH A:R5B1632 4.3 46.5 0.2 CAK A:R5B1632 4.3 47.7 0.2 CAF A:R5B1632 4.4 45.8 0.2 CAM A:R5B1632 4.4 47.0 0.2 NBA A:R5A1631 4.4 49.5 0.2 HBH A:R5A1631 4.5 48.0 0.2 CBB A:R5A1631 4.5 52.8 0.2 HAG A:R5A1631 4.6 48.9 0.2 HBC A:R5A1631 4.7 48.9 0.2 OE1 A:GLU102 4.7 47.6 1.0 HBD A:R5A1631 4.8 49.3 0.2 CBD A:R5B1632 4.8 45.5 0.2 CCD A:R5B1632 4.8 48.4 0.2 CBI A:R5B1632 4.8 45.2 0.2 CCI A:R5B1632 4.8 50.4 0.2 HBK A:R5A1631 4.8 45.2 0.2 CAC A:R5A1631 4.9 43.7 0.2 CA0 A:R5B1632 4.9 46.9 0.2 NAD A:R5A1631 4.9 44.5 0.2 CCD A:R5A1631 4.9 48.1 0.2 CAG A:R5B1632 4.9 46.5 0.2 CCC A:R5A1631 5.0 47.1 0.2

D.B.Langley, D.E.Brown, L.E.Cheruzel, S.M.Contakes, A.P.Duff, K.M.Hilmer, D.M.Dooley, H.B.Gray, J.M.Guss, H.C.Freeman. Enantiomer-Specific Binding of Ruthenium(II) Molecular Wires By the Amine Oxidase of Arthrobacter Globiformis. J. Am. Chem. Soc. V. 130 8069 2008.
ISSN: ESSN 1520-5126
PubMed: 18507382
DOI: 10.1021/JA801289F