4OKA

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

Summary for 4OKA

Entry DOI	10.2210/pdb4oka/pdb
Descriptor	Streptavidin, [N-(4-{[2-(amino-kappaN)ethyl]sulfamoyl-kappaN}phenyl)-5-(2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanamidato]iridium(III), IRIDIUM ION, ... (4 entities in total)
Functional Keywords	beta barrel, transfer hydrogenation, iridium piano stool, biotin-binding protein
Biological source	Streptomyces avidinii
Cellular location	Secreted: P22629
Total number of polymer chains	1
Total formula weight	17437.11
Authors	Schirmer, T.,Heinisch, T. (deposition date: 2014-01-22, release date: 2014-11-05, Last modification date: 2023-11-08)
Primary citation	Robles, V.M.,Durrenberger, M.,Heinisch, T.,Lledos, A.,Schirmer, T.,Ward, T.R.,Marechal, J.D. Structural, Kinetic, and Docking Studies of Artificial Imine Reductases Based on Biotin-Streptavidin Technology: An Induced Lock-and-Key Hypothesis J.Am.Chem.Soc., 136:15676-15683, 2014 Cited by PubMed: 25317660 DOI: 10.1021/ja508258t PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.505 Å)

Structure validation