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Structure paper

TitleStructural, Kinetic, and Docking Studies of Artificial Imine Reductases Based on Biotin-Streptavidin Technology: An Induced Lock-and-Key Hypothesis
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 136, Page 15676-15683, Year 2014
Publish dateJan 22, 2014 (structure data deposition date)
AuthorsRobles, V.M. / Durrenberger, M. / Heinisch, T. / Lledos, A. / Schirmer, T. / Ward, T.R. / Marechal, J.D.
External linksJ. Am. Chem. Soc. / PubMed:25317660
MethodsX-ray diffraction
Resolution2.505 Å
Structure data

PDB-4oka:
Structural-, Kinetic- and Docking Studies of Artificial Imine Reductases Based on the Biotin-Streptavidin Technology: An Induced Lock-and-Key Hypothesis
Method: X-RAY DIFFRACTION / Resolution: 2.505 Å

Chemicals

ChemComp-5IR:
[N-(4-{[2-(amino-kappaN)ethyl]sulfamoyl-kappaN}phenyl)-5-(2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanamidato]iridium(III)

ChemComp-IR:
Unknown entry

ChemComp-HOH:
WATER

Source
  • streptomyces avidinii (bacteria)
KeywordsBIOTIN-BINDING PROTEIN / beta barrel / transfer hydrogenation / iridium piano stool

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