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: 25317660DOI: 10.1021/ja508258t PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.505 Å) |
Structure validation
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