Iridium in PDB 6ess: Artificial Imine Reductase Mutant S112A-N118P-K121A-S122M

The structure of Artificial Imine Reductase Mutant S112A-N118P-K121A-S122M, PDB code: 6ess was solved by M.Hestericova, T.Heinisch, L.Alonso-Cotchico, J.-D.Marechal, P.Vidossich, T.R.Ward, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.30 / 1.91
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	58.079, 58.079, 185.125, 90.00, 90.00, 90.00
R / Rfree (%)	27.6 / 32.7

The binding sites of Iridium atom in the Artificial Imine Reductase Mutant S112A-N118P-K121A-S122M (pdb code 6ess). This binding sites where shown within 5.0 Angstroms radius around Iridium atom.
In total 4 binding sites of Iridium where determined in the Artificial Imine Reductase Mutant S112A-N118P-K121A-S122M, PDB code: 6ess:
Jump to Iridium binding site number: 1; 2; 3; 4;

Iridium binding site 1 out of 4 in the Artificial Imine Reductase Mutant S112A-N118P-K121A-S122M


Mono view


Stereo pair view

A full contact list of Iridium with other atoms in the Ir binding site number 1 of Artificial Imine Reductase Mutant S112A-N118P-K121A-S122M within 5.0Å range: probe atom residue distance (Å) B Occ A:Ir400 b:92.9 occ:1.00 IR1 A:4IR400 0.0 92.9 1.0 N5 A:4IR400 2.1 98.7 1.0 N4 A:4IR400 2.1 81.4 1.0 C17 A:4IR400 2.1 0.6 1.0 C18 A:4IR400 2.1 0.3 1.0 C21 A:4IR400 2.1 0.0 1.0 C19 A:4IR400 2.1 0.2 1.0 C20 A:4IR400 2.1 0.0 1.0 C28 A:4IR400 3.0 77.5 1.0 C27 A:4IR400 3.0 79.6 1.0 S2 A:4IR400 3.2 50.6 1.0 C22 A:4IR400 3.3 0.7 1.0 C23 A:4IR400 3.3 0.0 1.0 C26 A:4IR400 3.3 99.4 1.0 C24 A:4IR400 3.3 88.6 1.0 C25 A:4IR400 3.3 87.0 1.0 O3 A:4IR400 3.4 41.1 1.0 O4 A:4IR400 3.6 43.8 1.0 O A:ALA121 4.5 48.1 1.0 C16 A:4IR400 4.7 43.3 1.0

Iridium binding site 2 out of 4 in the Artificial Imine Reductase Mutant S112A-N118P-K121A-S122M


Mono view


Stereo pair view

A full contact list of Iridium with other atoms in the Ir binding site number 2 of Artificial Imine Reductase Mutant S112A-N118P-K121A-S122M within 5.0Å range: probe atom residue distance (Å) B Occ A:Ir401 b:75.2 occ:1.00 O A:HOH514 2.1 25.8 1.0 NE2 A:HIS87 2.6 25.3 1.0 CD2 A:HIS87 3.2 24.9 1.0 CE1 A:HIS87 3.7 28.4 1.0 CG A:HIS87 4.4 28.1 1.0 ND1 A:HIS87 4.6 28.3 1.0

Iridium binding site 3 out of 4 in the Artificial Imine Reductase Mutant S112A-N118P-K121A-S122M


Mono view


Stereo pair view

A full contact list of Iridium with other atoms in the Ir binding site number 3 of Artificial Imine Reductase Mutant S112A-N118P-K121A-S122M within 5.0Å range: probe atom residue distance (Å) B Occ A:Ir402 b:77.9 occ:1.00 O A:HOH509 2.5 39.4 1.0 NE2 A:HIS127 2.7 42.6 1.0 CD2 A:HIS127 3.2 35.6 1.0 CE1 A:HIS127 3.7 42.0 1.0 IR A:IR403 4.4 99.2 1.0 CG A:HIS127 4.4 31.9 1.0 ND1 A:HIS127 4.6 45.7 1.0

Iridium binding site 4 out of 4 in the Artificial Imine Reductase Mutant S112A-N118P-K121A-S122M


Mono view


Stereo pair view

A full contact list of Iridium with other atoms in the Ir binding site number 4 of Artificial Imine Reductase Mutant S112A-N118P-K121A-S122M within 5.0Å range: probe atom residue distance (Å) B Occ A:Ir403 b:99.2 occ:1.00 O A:HOH509 2.3 39.4 1.0 NE2 A:HIS127 3.2 42.6 1.0 CE1 A:HIS127 3.3 42.0 1.0 CD2 A:HIS127 4.3 35.6 1.0 ND1 A:HIS127 4.4 45.7 1.0 IR A:IR402 4.4 77.9 1.0 CG A:HIS127 4.9 31.9 1.0

M.Hestericova, T.Heinisch, L.Alonso-Cotchico, J.D.Marechal, P.Vidossich, T.R.Ward. Directed Evolution of An Artificial Imine Reductase. Angew. Chem. Int. Ed. Engl. V. 57 1863 2018.
ISSN: ESSN 1521-3773
PubMed: 29265726
DOI: 10.1002/ANIE.201711016