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
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1. Protein Identity and Related Structures Protein Identity & Related Structures
[N-(4-{[2-(amino-kappaN)ethyl]sulfamoyl-kappaN}phenyl)-5-(2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanamidato]iridium(III)
× 4
IRIDIUM ION
× 4
water
× 4
The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links.
Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.
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2. Structure Basics 2. Structure Basics
Entry ID entry_id
4oka
Deposition date deposition_date
2014-01-22
Structure title title
Structural-, Kinetic- and Docking Studies of Artificial Imine Reductases Based on the Biotin-Streptavidin Technology: An Induced Lock-and-Key Hypothesis
Keywords keywords
beta barrel, transfer hydrogenation, iridium piano stool, BIOTIN-BINDING PROTEIN; BIOTIN-BINDING PROTEIN
Experimental Method method
X-RAY DIFFRACTION
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3. Official assembly/model SAXS Official SAXS Profiles
This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.
4oka__assembly_1__model_1
Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)