Iridium in PDB 4oka: Structural-, Kinetic- and Docking Studies of Artificial Imine Reductases Based on the Biotin-Streptavidin Technology: An Induced Lock-and-Key Hypothesis

The structure of Structural-, Kinetic- and Docking Studies of Artificial Imine Reductases Based on the Biotin-Streptavidin Technology: An Induced Lock-and-Key Hypothesis, PDB code: 4oka was solved by T.Schirmer, T.Heinisch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.44 / 2.50
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	57.605, 57.605, 183.325, 90.00, 90.00, 90.00
R / Rfree (%)	19.8 / 24

The binding sites of Iridium atom in the Structural-, Kinetic- and Docking Studies of Artificial Imine Reductases Based on the Biotin-Streptavidin Technology: An Induced Lock-and-Key Hypothesis (pdb code 4oka). This binding sites where shown within 5.0 Angstroms radius around Iridium atom.
In total 3 binding sites of Iridium where determined in the Structural-, Kinetic- and Docking Studies of Artificial Imine Reductases Based on the Biotin-Streptavidin Technology: An Induced Lock-and-Key Hypothesis, PDB code: 4oka:
Jump to Iridium binding site number: 1; 2; 3;

Iridium binding site 1 out of 3 in the Structural-, Kinetic- and Docking Studies of Artificial Imine Reductases Based on the Biotin-Streptavidin Technology: An Induced Lock-and-Key Hypothesis


Mono view


Stereo pair view

A full contact list of Iridium with other atoms in the Ir binding site number 1 of Structural-, Kinetic- and Docking Studies of Artificial Imine Reductases Based on the Biotin-Streptavidin Technology: An Induced Lock-and-Key Hypothesis within 5.0Å range: probe atom residue distance (Å) B Occ A:Ir400 b:63.8 occ:0.60 IR A:5IR400 0.0 63.8 0.6 N4 A:5IR400 2.2 28.4 0.6 N5 A:5IR400 2.2 31.1 0.6 NZ A:LYS112 2.3 36.4 1.0 O3 A:5IR400 2.9 32.2 0.6 O3 A:5IR400 2.9 32.0 0.4 C27 A:5IR400 2.9 29.7 0.6 C28 A:5IR400 3.0 30.6 0.6 S2 A:5IR400 3.0 34.1 0.6 CE A:LYS112 3.3 29.1 1.0 O4 A:5IR400 3.3 29.8 0.4 O4 A:5IR400 3.5 29.7 0.6 S2 A:5IR400 3.7 31.3 0.4 CD A:LYS112 4.2 25.5 1.0 C16 A:5IR400 4.3 28.3 0.6 C16 A:5IR400 4.7 29.0 0.4 C13 A:5IR400 4.9 27.5 0.4 N4 A:5IR400 4.9 33.9 0.4

Iridium binding site 2 out of 3 in the Structural-, Kinetic- and Docking Studies of Artificial Imine Reductases Based on the Biotin-Streptavidin Technology: An Induced Lock-and-Key Hypothesis


Mono view


Stereo pair view

A full contact list of Iridium with other atoms in the Ir binding site number 2 of Structural-, Kinetic- and Docking Studies of Artificial Imine Reductases Based on the Biotin-Streptavidin Technology: An Induced Lock-and-Key Hypothesis within 5.0Å range: probe atom residue distance (Å) B Occ A:Ir400 b:73.2 occ:0.40 IR A:5IR400 0.0 73.2 0.4 N4 A:5IR400 2.2 33.9 0.4 N5 A:5IR400 2.2 34.3 0.4 O3 A:5IR400 2.9 32.0 0.4 O3 A:5IR400 2.9 32.2 0.6 C27 A:5IR400 3.0 31.3 0.4 C28 A:5IR400 3.0 32.0 0.4 S2 A:5IR400 3.1 31.3 0.4 O4 A:5IR400 3.9 29.8 0.4 S2 A:5IR400 4.2 34.1 0.6 C16 A:5IR400 4.3 29.0 0.4 O4 A:5IR400 4.6 29.7 0.6 C15 A:5IR400 4.7 28.1 0.6 C16 A:5IR400 4.9 28.3 0.6 C13 A:5IR400 5.0 27.5 0.4

Iridium binding site 3 out of 3 in the Structural-, Kinetic- and Docking Studies of Artificial Imine Reductases Based on the Biotin-Streptavidin Technology: An Induced Lock-and-Key Hypothesis


Mono view


Stereo pair view

A full contact list of Iridium with other atoms in the Ir binding site number 3 of Structural-, Kinetic- and Docking Studies of Artificial Imine Reductases Based on the Biotin-Streptavidin Technology: An Induced Lock-and-Key Hypothesis within 5.0Å range: probe atom residue distance (Å) B Occ A:Ir401 b:44.0 occ:0.30 NE2 A:HIS127 2.9 14.3 1.0 CD2 A:HIS127 3.5 14.4 1.0 CE1 A:HIS127 4.0 12.2 1.0 CG A:HIS127 4.8 12.5 1.0 ND1 A:HIS127 5.0 14.9 1.0

V.Munoz Robles, M.Durrenberger, T.Heinisch, A.Lledos, T.Schirmer, T.R.Ward, J.D.Marechal. Structural-, Kinetic- and Docking Studies of Artificial Imine Reductases Based on the Biotin-Streptavidin Technology: An Induced Lock-and-Key Hypothesis J.Am.Chem.Soc. 2014.
ISSN: ESSN 1520-5126
PubMed: 25317660
DOI: 10.1021/JA508258T